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Lyase (oxo-acid)
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PDB id
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1ctn
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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.14
- Chitinase.
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Reaction:
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Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.
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Gene Ontology (GO) functional annotation
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Biological process
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metabolic process
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4 terms
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Biochemical function
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catalytic activity
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6 terms
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DOI no:
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Structure
2:1169-1180
(1994)
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PubMed id:
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Crystal structure of a bacterial chitinase at 2.3 A resolution.
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A.Perrakis,
I.Tews,
Z.Dauter,
A.B.Oppenheim,
I.Chet,
K.S.Wilson,
C.E.Vorgias.
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ABSTRACT
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BACKGROUND: Chitinases cleave the beta-1-4-glycosidic bond between the
N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are
present in plants, bacteria and fungi, but whereas structures are available for
two prototypic plant enzymes, no structure is available for a bacterial or
fungal chitinase. RESULTS: To redress this imbalance, the structure of native
chitinase A from Serratia marcescens has been solved by multiple isomorphous
replacement and refined at 2.3 A resolution, resulting in a crystallographic
R-factor of 16.2%. The enzyme comprises three domains: an all beta-strand
amino-terminal domain, a catalytic alpha/beta-barrel domain, and a small
alpha+beta-fold domain. There are several residues with unusual geometries in
the structure. Structure determination of chitinase A in complex with
N,N',N",N"'-tetra-acetylo-chitotetraose, together with biochemical and
sequence analysis data, enabled the positions of the active-site and catalytic
residues to be proposed. CONCLUSIONS: The reaction mechanism seems to be similar
to that of lysozyme and most other glycosylhydrolases, i.e. general acid-base
catalysis. The role of the amino-terminal domain could not be identified, but it
has similarities to the fibronectin III domain. This domain may possibly
facilitate the interaction of chitinase A with chitin.
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Selected figure(s)
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Figure 8.
Figure 8. Difference density (F[o]–F[c] , with phases from
the native model) clearly showing the bound NAG. The active-site
residues are shown. Density is contoured at the 4σ level. The
orientation of the ring is not clear, and it is modelled in the
most likely position according to chemical knowledge of the
reaction mechanism, as described in the text. The role of water
181 is unclear. It is presented here to show the interpretation
of this density. Figure drawn using O/OPLOT [39]. Figure 8.
Difference density (F[o]–F[c] , with phases from the native
model) clearly showing the bound NAG. The active-site residues
are shown. Density is contoured at the 4σ level. The
orientation of the ring is not clear, and it is modelled in the
most likely position according to chemical knowledge of the
reaction mechanism, as described in the text. The role of water
181 is unclear. It is presented here to show the interpretation
of this density. Figure drawn using O/OPLOT [[3]39].
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Figure 11.
Figure 11. Stereo representation of the active site of ChiA.
Carbons are drawn in black, oxygens in red and nitrogens in
blue. Details for the proposed mechanism are given in the text.
Figure 11. Stereo representation of the active site of ChiA.
Carbons are drawn in black, oxygens in red and nitrogens in
blue. Details for the proposed mechanism are given in the text.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1994,
2,
1169-1180)
copyright 1994.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
|
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| |
PubMed id
|
|
Reference
|
|
|
|
|
|
Y.Wu,
F.Liu,
Y.C.Liu,
Z.H.Zhang,
T.T.Zhou,
X.Liu,
Q.R.Shen,
and
B.Shen
(2011).
Identification of chitinases Is-chiA and Is-chiB from Isoptericola jiangsuensis CLG and their characterization.
|
| |
Appl Microbiol Biotechnol, 89,
705-713.
|
|
|
|
|
|
|
H.Li,
and
L.H.Greene
(2010).
Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
|
| |
PLoS One, 5,
e8654.
|
|
|
|
|
|
|
H.Tsuji,
S.Nishimura,
T.Inui,
Y.Kado,
K.Ishikawa,
T.Nakamura,
and
K.Uegaki
(2010).
Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site.
|
| |
FEBS J, 277,
2683-2695.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
S.Kumar,
N.Singh,
B.Mishra,
D.Dube,
M.Sinha,
S.B.Singh,
S.Dey,
P.Kaur,
S.Sharma,
and
T.P.Singh
(2010).
Modulation of inhibitory activity of xylanase-α-amylase inhibitor protein (XAIP): binding studies and crystal structure determination of XAIP-II from Scadoxus multiflorus at 1.2 Šresolution.
|
| |
BMC Struct Biol, 10,
41.
|
|
|
|
|
|
|
S.Kumar,
N.Singh,
M.Sinha,
D.Dube,
S.B.Singh,
A.Bhushan,
P.Kaur,
A.Srinivasan,
S.Sharma,
and
T.P.Singh
(2010).
Crystal structure determination and inhibition studies of a novel xylanase and alpha-amylase inhibitor protein (XAIP) from Scadoxus multiflorus.
|
| |
FEBS J, 277,
2868-2882.
|
|
|
|
|
|
|
Y.Kezuka,
M.Kojima,
R.Mizuno,
K.Suzuki,
T.Watanabe,
and
T.Nonaka
(2010).
Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering.
|
| |
Proteins, 78,
2295-2305.
|
|
|
PDB code:
|
|
|
|
|
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|
|
A.B.Duzhak,
Z.I.Panfilova,
T.G.Duzhak,
and
E.A.Vasyunina
(2009).
Extracellular chitinases of mutant superproducing strain Serratia marcescens M-1.
|
| |
Biochemistry (Mosc), 74,
209-214.
|
|
|
|
|
|
|
F.P.Lin,
H.H.Chuang,
Y.H.Liu,
C.Y.Hsieh,
P.W.Lin,
and
H.Y.Lin
(2009).
Effects of C-terminal amino acids truncation on enzyme properties of Aeromonas caviae D1 chitinase.
|
| |
Arch Microbiol, 191,
265-273.
|
|
|
|
|
|
|
H.Zakariassen,
B.B.Aam,
S.J.Horn,
K.M.Vårum,
M.Sørlie,
and
V.G.Eijsink
(2009).
Aromatic Residues in the Catalytic Center of Chitinase A from Serratia marcescens Affect Processivity, Enzyme Activity, and Biomass Converting Efficiency.
|
| |
J Biol Chem, 284,
10610-10617.
|
|
|
|
|
|
|
K.Eurich,
M.Segawa,
S.Toei-Shimizu,
and
E.Mizoguchi
(2009).
Potential role of chitinase 3-like-1 in inflammation-associated carcinogenic changes of epithelial cells.
|
| |
World J Gastroenterol, 15,
5249-5259.
|
|
|
|
|
|
|
S.A.Mostafa,
M.S.Mahmoud,
Z.K.Mohamed,
and
M.R.Enan
(2009).
Cloning and molecular characterization of chitinase from Bacillus licheniformis MS-3.
|
| |
J Gen Appl Microbiol, 55,
241-246.
|
|
|
|
|
|
|
S.Kudan,
and
R.Pichyangkura
(2009).
Purification and characterization of thermostable chitinase from Bacillus licheniformis SK-1.
|
| |
Appl Biochem Biotechnol, 157,
23-35.
|
|
|
|
|
|
|
W.Suginta,
S.Pantoom,
and
H.Prinz
(2009).
Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi.
|
| |
J Chem Biol, 2,
191-202.
|
|
|
|
|
|
|
B.Synstad,
G.Vaaje-Kolstad,
F.H.Cederkvist,
S.F.Saua,
S.J.Horn,
V.G.Eijsink,
and
M.Sørlie
(2008).
Expression and characterization of endochitinase C from Serratia marcescens BJL200 and its purification by a one-step general chitinase purification method.
|
| |
Biosci Biotechnol Biochem, 72,
715-723.
|
|
|
|
|
|
|
C.Petter,
C.Scholz,
H.Wessner,
G.Hansen,
P.Henklein,
T.Watanabe,
and
W.Höhne
(2008).
Phage display screening for peptidic chitinase inhibitors.
|
| |
J Mol Recognit, 21,
401-409.
|
|
|
|
|
|
|
E.Stefanidi,
and
C.E.Vorgias
(2008).
Molecular analysis of the gene encoding a new chitinase from the marine psychrophilic bacterium Moritella marina and biochemical characterization of the recombinant enzyme.
|
| |
Extremophiles, 12,
541-552.
|
|
|
|
|
|
|
G.Y.Zhao,
X.L.Chen,
H.L.Zhao,
B.B.Xie,
B.C.Zhou,
and
Y.Z.Zhang
(2008).
Hydrolysis of Insoluble Collagen by Deseasin MCP-01 from Deep-sea Pseudoalteromonas sp. SM9913: COLLAGENOLYTIC CHARACTERS, COLLAGEN-BINDING ABILITY OF C-TERMINAL POLYCYSTIC KIDNEY DISEASE DOMAIN, AND IMPLICATION FOR ITS NOVEL ROLE IN DEEP-SEA SEDIMENTARY PARTICULATE ORGANIC NITROGEN DEGRADATION.
|
| |
J Biol Chem, 283,
36100-36107.
|
|
|
|
|
|
|
H.H.Chuang,
H.Y.Lin,
and
F.P.Lin
(2008).
Biochemical characteristics of C-terminal region of recombinant chitinase from Bacillus licheniformis: implication of necessity for enzyme properties.
|
| |
FEBS J, 275,
2240-2254.
|
|
|
|
|
|
|
S.Pantoom,
C.Songsiriritthigul,
and
W.Suginta
(2008).
The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A.
|
| |
BMC Biochem, 9,
2.
|
|
|
|
|
|
|
V.G.Eijsink,
G.Vaaje-Kolstad,
K.M.Vårum,
and
S.J.Horn
(2008).
Towards new enzymes for biofuels: lessons from chitinase research.
|
| |
Trends Biotechnol, 26,
228-235.
|
|
|
|
|
|
|
Z.H.Liu,
Q.Yang,
S.Hu,
J.D.Zhang,
and
J.Ma
(2008).
Cloning and characterization of a novel chitinase gene (chi46) from Chaetomium globosum and identification of its biological activity.
|
| |
Appl Microbiol Biotechnol, 80,
241-252.
|
|
|
|
|
|
|
H.H.Chuang,
and
F.P.Lin
(2007).
New role of C-terminal 30 amino acids on the insoluble chitin hydrolysis in actively engineered chitinase from Vibrio parahaemolyticus.
|
| |
Appl Microbiol Biotechnol, 76,
123-133.
|
|
|
|
|
|
|
H.S.Kim,
K.N.Timmis,
and
P.N.Golyshin
(2007).
Characterization of a chitinolytic enzyme from Serratia sp. KCK isolated from kimchi juice.
|
| |
Appl Microbiol Biotechnol, 75,
1275-1283.
|
|
|
|
|
|
|
R.Hurtado-Guerrero,
and
D.M.van Aalten
(2007).
Structure of Saccharomyces cerevisiae chitinase 1 and screening-based discovery of potent inhibitors.
|
| |
Chem Biol, 14,
589-599.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
T.Nakamura,
S.Mine,
Y.Hagihara,
K.Ishikawa,
and
K.Uegaki
(2007).
Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun, 63,
7.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
Y.Kwon,
S.H.Kim,
M.S.Jung,
M.S.Kim,
J.E.Oh,
H.W.Ju,
K.I.Kim,
E.Vierling,
H.Lee,
and
S.W.Hong
(2007).
Arabidopsis hot2 encodes an endochitinase-like protein that is essential for tolerance to heat, salt and drought stresses.
|
| |
Plant J, 49,
184-193.
|
|
|
|
|
|
|
Zaheer-ul-Haq,
P.Dalal,
N.N.Aronson,
and
J.D.Madura
(2007).
Family 18 chitolectins: comparison of MGP40 and HUMGP39.
|
| |
Biochem Biophys Res Commun, 359,
221-226.
|
|
|
|
|
|
|
A.W.Schüttelkopf,
O.A.Andersen,
F.V.Rao,
M.Allwood,
C.Lloyd,
I.M.Eggleston,
and
D.M.van Aalten
(2006).
Screening-based discovery and structural dissection of a novel family 18 chitinase inhibitor.
|
| |
J Biol Chem, 281,
27278-27285.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
H.F.Bigg,
R.Wait,
A.D.Rowan,
and
T.E.Cawston
(2006).
The mammalian chitinase-like lectin, YKL-40, binds specifically to type I collagen and modulates the rate of type I collagen fibril formation.
|
| |
J Biol Chem, 281,
21082-21095.
|
|
|
|
|
|
|
K.E.Kabir,
D.Hirowatari,
K.Watanabe,
and
D.Koga
(2006).
Purification and characterization of a novel isozyme of chitinase from Bombyx mori.
|
| |
Biosci Biotechnol Biochem, 70,
252-262.
|
|
|
|
|
|
|
M.Ike,
K.Nagamatsu,
A.Shioya,
M.Nogawa,
W.Ogasawara,
H.Okada,
and
Y.Morikawa
(2006).
Purification, characterization, and gene cloning of 46 kDa chitinase (Chi46) from Trichoderma reesei PC-3-7 and its expression in Escherichia coli.
|
| |
Appl Microbiol Biotechnol, 71,
294-303.
|
|
|
|
|
|
|
N.N.Aronson,
B.A.Halloran,
M.F.Alexeyev,
X.E.Zhou,
Y.Wang,
E.J.Meehan,
and
L.Chen
(2006).
Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.
|
| |
Biosci Biotechnol Biochem, 70,
243-251.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
R.Stern,
and
M.J.Jedrzejas
(2006).
Hyaluronidases: their genomics, structures, and mechanisms of action.
|
| |
Chem Rev, 106,
818-839.
|
|
|
|
|
|
|
S.J.Horn,
A.Sørbotten,
B.Synstad,
P.Sikorski,
M.Sørlie,
K.M.Vårum,
and
V.G.Eijsink
(2006).
Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens.
|
| |
FEBS J, 273,
491-503.
|
|
|
|
|
|
|
S.M.Bonfim,
A.H.Cruz,
R.S.Jesuino,
C.J.Ulhoa,
E.E.Molinari-Madlum,
C.M.Soares,
and
M.Pereira
(2006).
Chitinase from Paracoccidioides brasiliensis: molecular cloning, structural, phylogenetic, expression and activity analysis.
|
| |
FEMS Immunol Med Microbiol, 46,
269-283.
|
|
|
|
|
|
|
S.Pyrpassopoulos,
M.Vlassi,
A.Tsortos,
Y.Papanikolau,
K.Petratos,
C.E.Vorgias,
and
G.Nounesis
(2006).
Equilibrium heat-induced denaturation of chitinase 40 from Streptomyces thermoviolaceus.
|
| |
Proteins, 64,
513-523.
|
|
|
|
|
|
|
T.Kawase,
S.Yokokawa,
A.Saito,
T.Fujii,
N.Nikaidou,
K.Miyashita,
and
T.Watanabe
(2006).
Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from S. coelicolor A3(2).
|
| |
Biosci Biotechnol Biochem, 70,
988-998.
|
|
|
|
|
|
|
X.Lan,
X.Zhang,
J.Hu,
and
M.Shimosaka
(2006).
Cloning, expression, and characterization of a chitinase from the chitinolytic bacterium Aeromonas hydrophila strain SUWA-9.
|
| |
Biosci Biotechnol Biochem, 70,
2437-2442.
|
|
|
|
|
|
|
A.L.Lovering,
S.S.Lee,
Y.W.Kim,
S.G.Withers,
and
N.C.Strynadka
(2005).
Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate.
|
| |
J Biol Chem, 280,
2105-2115.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
F.Driss,
M.Kallassy-Awad,
N.Zouari,
and
S.Jaoua
(2005).
Molecular characterization of a novel chitinase from Bacillus thuringiensis subsp. kurstaki.
|
| |
J Appl Microbiol, 99,
945-953.
|
|
|
|
|
|
|
F.V.Rao,
O.A.Andersen,
K.A.Vora,
J.A.Demartino,
and
D.M.van Aalten
(2005).
Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes.
|
| |
Chem Biol, 12,
973-980.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
G.Vaaje-Kolstad,
D.R.Houston,
A.H.Riemen,
V.G.Eijsink,
and
D.M.van Aalten
(2005).
Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21.
|
| |
J Biol Chem, 280,
11313-11319.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
H.Orikoshi,
S.Nakayama,
C.Hanato,
K.Miyamoto,
and
H.Tsujibo
(2005).
Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7.
|
| |
J Appl Microbiol, 99,
551-557.
|
|
|
|
|
|
|
M.B.Joshi,
M.E.Rogers,
A.M.Shakarian,
M.Yamage,
S.A.Al-Harthi,
P.A.Bates,
and
D.M.Dwyer
(2005).
Molecular characterization, expression, and in vivo analysis of LmexCht1: the chitinase of the human pathogen, Leishmania mexicana.
|
| |
J Biol Chem, 280,
3847-3861.
|
|
|
|
|
|
|
M.J.Jedrzejas,
and
R.Stern
(2005).
Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis.
|
| |
Proteins, 61,
227-238.
|
|
|
|
|
|
|
Q.Li,
F.Wang,
Y.Zhou,
and
X.Xiao
(2005).
Putative exposed aromatic and hydroxyl residues on the surface of the N-terminal domains of Chi1 from Aeromonas caviae CB101 are essential for chitin binding and hydrolysis.
|
| |
Appl Environ Microbiol, 71,
7559-7561.
|
|
|
|
|
|
|
V.Seidl,
B.Huemer,
B.Seiboth,
and
C.P.Kubicek
(2005).
A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases.
|
| |
FEBS J, 272,
5923-5939.
|
|
|
|
|
|
|
W.Suginta,
A.Vongsuwan,
C.Songsiriritthigul,
J.Svasti,
and
H.Prinz
(2005).
Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS.
|
| |
FEBS J, 272,
3376-3386.
|
|
|
|
|
|
|
B.Synstad,
S.Gåseidnes,
D.M.Van Aalten,
G.Vriend,
J.E.Nielsen,
and
V.G.Eijsink
(2004).
Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase.
|
| |
Eur J Biochem, 271,
253-262.
|
|
|
|
|
|
|
E.Devillard,
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R.Lamed,
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Ruminococcus albus 8 mutants defective in cellulose degradation are deficient in two processive endocellulases, Cel48A and Cel9B, both of which possess a novel modular architecture.
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J Bacteriol, 186,
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M.Mizuno,
T.Tonozuka,
S.Suzuki,
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S.Kamitori,
A.Nishikawa,
and
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Structural insights into substrate specificity and function of glucodextranase.
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J Biol Chem, 279,
10575-10583.
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PDB codes:
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T.Kawase,
A.Saito,
T.Sato,
R.Kanai,
T.Fujii,
N.Nikaidou,
K.Miyashita,
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Distribution and phylogenetic analysis of family 19 chitinases in Actinobacteria.
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Appl Environ Microbiol, 70,
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A.K.Mohanty,
G.Singh,
M.Paramasivam,
K.Saravanan,
T.Jabeen,
S.Sharma,
S.Yadav,
P.Kaur,
P.Kumar,
A.Srinivasan,
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Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution.
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J Biol Chem, 278,
14451-14460.
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PDB code:
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D.R.Houston,
A.D.Recklies,
J.C.Krupa,
and
D.M.van Aalten
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Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes.
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J Biol Chem, 278,
30206-30212.
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PDB codes:
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F.Fusetti,
T.Pijning,
K.H.Kalk,
E.Bos,
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Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39.
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J Biol Chem, 278,
37753-37760.
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PDB codes:
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F.P.Wang,
Q.Li,
Y.Zhou,
M.G.Li,
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The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis.
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Proteins, 53,
908-916.
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J.Gao,
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K.R.Shockley,
M.A.Pysz,
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Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases.
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Appl Environ Microbiol, 69,
3119-3128.
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M.Ueda,
M.Kojima,
T.Yoshikawa,
N.Mitsuda,
K.Araki,
T.Kawaguchi,
K.Miyatake,
M.Arai,
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A novel type of family 19 chitinase from Aeromonas sp. No.10S-24. Cloning, sequence, expression, and the enzymatic properties.
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Eur J Biochem, 270,
2513-2520.
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T.Uchiyama,
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J.Yamaguchi,
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T.Yanagida,
N.Nikaidou,
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Uptake of N,N'-diacetylchitobiose [(GlcNAc)2] via the phosphotransferase system is essential for chitinase production by Serratia marcescens 2170.
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J Bacteriol, 185,
1776-1782.
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Y.Itoh,
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H.Takizawa,
N.Nikaidou,
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H.Nishihashi,
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Family 19 chitinase of Streptomyces griseus HUT6037 increases plant resistance to the fungal disease.
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Biosci Biotechnol Biochem, 67,
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Y.Papanikolau,
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De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.
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Acta Crystallogr D Biol Crystallogr, 59,
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PDB codes:
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B.M.Abdel-Banat,
W.Zhou,
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and
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Analysis of hydrolytic activity of a 65-kDa chitinase from the silkworm, Bombyx mori.
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Biosci Biotechnol Biochem, 66,
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F.Fusetti,
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H.J.Rozeboom,
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R.G.Boot,
J.M.Aerts,
and
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(2002).
Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins.
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J Biol Chem, 277,
25537-25544.
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PDB codes:
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K.Miyamoto,
E.Nukui,
M.Hirose,
F.Nagai,
T.Sato,
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A metalloprotease (MprIII) involved in the chitinolytic system of a marine bacterium, Alteromonas sp. strain O-7.
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Appl Environ Microbiol, 68,
5563-5570.
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K.Suzuki,
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M.Suzuki,
T.Uchiyama,
F.Katouno,
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Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation.
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Biosci Biotechnol Biochem, 66,
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P.F.Varela,
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R.A.Mariuzza,
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Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster.
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J Biol Chem, 277,
13229-13236.
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PDB codes:
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Y.Itoh,
T.Kawase,
N.Nikaidou,
H.Fukada,
M.Mitsutomi,
T.Watanabe,
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Functional analysis of the chitin-binding domain of a family 19 chitinase from Streptomyces griseus HUT6037: substrate-binding affinity and cis-dominant increase of antifungal function.
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Biosci Biotechnol Biochem, 66,
1084-1092.
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D.Jablonowski,
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F.Meinhardt,
M.J.Stark,
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Saccharomyces cerevisiae cell wall chitin, the Kluyveromyces lactis zymocin receptor.
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Yeast, 18,
1285-1299.
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D.M.van Aalten,
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B.Synstad,
S.Gåseidnes,
M.G.Peter,
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Structural insights into the catalytic mechanism of a family 18 exo-chitinase.
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Proc Natl Acad Sci U S A, 98,
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PDB codes:
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H.Kogelberg,
and
T.Feizi
(2001).
New structural insights into lectin-type proteins of the immune system.
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Curr Opin Struct Biol, 11,
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J.T.Dessens,
J.Mendoza,
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J.M.Vinetz,
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Knockout of the rodent malaria parasite chitinase pbCHT1 reduces infectivity to mosquitoes.
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Infect Immun, 69,
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K.Suzuki,
T.Uchiyama,
M.Suzuki,
N.Nikaidou,
M.Regue,
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LysR-type transcriptional regulator ChiR is essential for production of all chitinases and a chitin-binding protein, CBP21, in Serratia marcescens 2170.
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Biosci Biotechnol Biochem, 65,
338-347.
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M.L.Wu,
Y.C.Chuang,
J.P.Chen,
C.S.Chen,
and
M.C.Chang
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Identification and characterization of the three chitin-binding domains within the multidomain chitinase Chi92 from Aeromonas hydrophila JP101.
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Appl Environ Microbiol, 67,
5100-5106.
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P.P.van der Holst,
H.R.Schlaman,
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Proteins involved in the production and perception of oligosaccharides in relation to plant and animal development.
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Curr Opin Struct Biol, 11,
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S.E.Thompson,
M.Smith,
M.C.Wilkinson,
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Identification and characterization of a chitinase antigen from Pseudomonas aeruginosa strain 385.
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Appl Environ Microbiol, 67,
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T.Lonhienne,
K.Mavromatis,
C.E.Vorgias,
L.Buchon,
C.Gerday,
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Cloning, sequences, and characterization of two chitinase genes from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes.
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J Bacteriol, 183,
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V.Chazalet,
K.Uehara,
R.A.Geremia,
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Identification of essential amino acids in the Azorhizobium caulinodans fucosyltransferase NodZ.
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J Bacteriol, 183,
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Y.Wu,
G.Egerton,
A.P.Underwood,
S.Sakuda,
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Expression and secretion of a larval-specific chitinase (family 18 glycosyl hydrolase) by the infective stages of the parasitic nematode, Onchocerca volvulus.
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J Biol Chem, 276,
42557-42564.
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D.C.Irwin,
S.Zhang,
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(2000).
Cloning, expression and characterization of a family 48 exocellulase, Cel48A, from Thermobifida fusca.
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Eur J Biochem, 267,
4988-4997.
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D.M.van Aalten,
B.Synstad,
M.B.Brurberg,
E.Hough,
B.W.Riise,
V.G.Eijsink,
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(2000).
Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution.
|
| |
Proc Natl Acad Sci U S A, 97,
5842-5847.
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PDB code:
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|
H.Tsujibo,
N.Hatano,
H.Endo,
K.Miyamoto,
and
Y.Inamori
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Purification and characterization of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520 and cloning of the encoding gene.
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Biosci Biotechnol Biochem, 64,
96.
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M.Hahn,
M.Hennig,
B.Schlesier,
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W.Höhne
(2000).
Structure of jack bean chitinase.
|
| |
Acta Crystallogr D Biol Crystallogr, 56,
1096-1099.
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PDB code:
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|
|
|
|
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|
|
M.Owhashi,
H.Arita,
and
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(2000).
Identification of a novel eosinophil chemotactic cytokine (ECF-L) as a chitinase family protein.
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J Biol Chem, 275,
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S.Cottaz,
B.Brasme,
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A fluorescence-quenched chitopentaose for the study of endo-chitinases and chitobiosidases.
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Eur J Biochem, 267,
5593-5600.
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T.Hollis,
A.F.Monzingo,
K.Bortone,
S.Ernst,
R.Cox,
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(2000).
The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis.
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| |
Protein Sci, 9,
544-551.
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PDB code:
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|
|
|
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|
T.Ikegami,
T.Okada,
M.Hashimoto,
S.Seino,
T.Watanabe,
and
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(2000).
Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1.
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| |
J Biol Chem, 275,
13654-13661.
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PDB code:
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W.Suginta,
P.A.Robertson,
B.Austin,
S.C.Fry,
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Chitinases from Vibrio: activity screening and purification of chiA from Vibrio carchariae.
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J Appl Microbiol, 89,
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Z.Marković-Housley,
G.Miglierini,
L.Soldatova,
P.J.Rizkallah,
U.Müller,
and
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(2000).
Crystal structure of hyaluronidase, a major allergen of bee venom.
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| |
Structure, 8,
1025-1035.
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PDB codes:
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|
D.H.Juers,
R.E.Huber,
and
B.W.Matthews
(1999).
Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases.
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| |
Protein Sci, 8,
122-136.
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J.M.Vinetz,
S.K.Dave,
C.A.Specht,
K.A.Brameld,
B.Xu,
R.Hayward,
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(1999).
The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences.
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| |
Proc Natl Acad Sci U S A, 96,
14061-14066.
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J.Saito,
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Y.Higuchi,
Y.Nagata,
A.Ando,
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(1999).
Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism.
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| |
J Biol Chem, 274,
30818-30825.
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PDB code:
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|
N.Nagano,
E.G.Hutchinson,
and
J.M.Thornton
(1999).
Barrel structures in proteins: automatic identification and classification including a sequence analysis of TIM barrels.
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Protein Sci, 8,
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N.O.Keyhani,
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Physiological aspects of chitin catabolism in marine bacteria.
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Biochim Biophys Acta, 1473,
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T.Tanaka,
S.Fujiwara,
S.Nishikori,
T.Fukui,
M.Takagi,
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A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1.
|
| |
Appl Environ Microbiol, 65,
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|
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C.J.Thomas,
H.L.Brown,
C.R.Hawes,
B.Y.Lee,
M.K.Min,
L.A.King,
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Localization of a baculovirus-induced chitinase in the insect cell endoplasmic reticulum.
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J Virol, 72,
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F.M.Vellieux
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A comparison of two algorithms for electron-density map improvement by introduction of atomicity: skeletonization, and map sorting followed by refinement.
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Acta Crystallogr D Biol Crystallogr, 54,
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H.Tsujibo,
H.Orikoshi,
K.Shiotani,
M.Hayashi,
J.Umeda,
K.Miyamoto,
C.Imada,
Y.Okami,
and
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(1998).
Characterization of chitinase C from a marine bacterium, Alteromonas sp. strain O-7, and its corresponding gene and domain structure.
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Appl Environ Microbiol, 64,
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K.Suzuki,
M.Suzuki,
M.Taiyoji,
N.Nikaidou,
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Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170.
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| |
Biosci Biotechnol Biochem, 62,
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R.Cohen-Kupiec,
and
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The molecular biology of chitin digestion.
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Curr Opin Biotechnol, 9,
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R.G.Boot,
G.H.Renkema,
M.Verhoek,
A.Strijland,
J.Bliek,
T.M.de Meulemeester,
M.M.Mannens,
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The human chitotriosidase gene. Nature of inherited enzyme deficiency.
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J Biol Chem, 273,
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T.Hollis,
A.F.Monzingo,
K.Bortone,
E.Schelp,
R.Cox,
and
J.D.Robertus
(1998).
Crystallization and preliminary X-ray analysis of a chitinase from the fungal pathogen Coccidioides immitis.
|
| |
Acta Crystallogr D Biol Crystallogr, 54,
1412-1413.
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C.S.Bond,
P.R.Clements,
S.J.Ashby,
C.A.Collyer,
S.J.Harrop,
J.J.Hopwood,
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Structure of a human lysosomal sulfatase.
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| |
Structure, 5,
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PDB code:
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|
K.D.Spindler,
M.Spindler-Barth,
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Effect of demethylation on the chitinase inhibitory activity of allosamidin.
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| |
Arch Insect Biochem Physiol, 36,
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K.Morimoto,
S.Karita,
T.Kimura,
K.Sakka,
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Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain.
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J Bacteriol, 179,
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L.S.Chernin,
L.De la Fuente,
V.Sobolev,
S.Haran,
C.E.Vorgias,
A.B.Oppenheim,
and
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Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans.
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Appl Environ Microbiol, 63,
834-839.
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T.Watanabe,
K.Kimura,
T.Sumiya,
N.Nikaidou,
K.Suzuki,
M.Suzuki,
M.Taiyoji,
S.Ferrer,
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Genetic analysis of the chitinase system of Serratia marcescens 2170.
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J Bacteriol, 179,
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C.E.Vorgias,
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Structure-function studies on the chitinolytic enzymes of Serratia marcescens chitinase and chitobiase.
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Ann N Y Acad Sci, 799,
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I.Tews,
A.Perrakis,
A.Oppenheim,
Z.Dauter,
K.S.Wilson,
and
C.E.Vorgias
(1996).
Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease.
|
| |
Nat Struct Biol, 3,
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|
PDB codes:
|
|
|
|
|
|
|
|
R.A.Warren
(1996).
Microbial hydrolysis of polysaccharides.
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Annu Rev Microbiol, 50,
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Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?
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Protein Sci, 5,
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T.Ohno,
S.Armand,
T.Hata,
N.Nikaidou,
B.Henrissat,
M.Mitsutomi,
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A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037.
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J Bacteriol, 178,
5065-5070.
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G.Davies,
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Structures and mechanisms of glycosyl hydrolases.
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Structure, 3,
853-859.
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|
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T.Barrett,
C.G.Suresh,
S.P.Tolley,
E.J.Dodson,
and
M.A.Hughes
(1995).
The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase.
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Structure, 3,
951-960.
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PDB code:
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Y.Sitrit,
C.E.Vorgias,
I.Chet,
and
A.B.Oppenheim
(1995).
Cloning and primary structure of the chiA gene from Aeromonas caviae.
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J Bacteriol, 177,
4187-4189.
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The most recent references are shown first.
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only a partial list as not all journals are covered by
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
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shown on the right.
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Links
