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Hydrolase PDB id
1llo
Jmol
Contents
Protein chain
273 a.a. *
Ligands
NAA-NAA-AMI
Waters ×189
* Residue conservation analysis
PDB id:
1llo
Name: Hydrolase
Title: Hevamine a (a plant endochitinase/lysozyme) complexed with allosamidin
Structure: Hevamine. Chain: a. Synonym: chitinase/lysozyme. Ec: 3.2.1.14, 3.2.1.17
Source: Hevea brasiliensis. Organism_taxid: 3981. Tissue: latex
Resolution:
1.85Å     R-factor:   0.146     R-free:   0.200
Authors: A.C.Terwisscha Van Scheltinga,S.Armand,K.H.Kalk,A.Isogai, B.Henrissat,B.W.Dijkstra
Key ref:
A.C.Terwisscha van Scheltinga et al. (1995). Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry, 34, 15619-15623. PubMed id: 7495789 DOI: 10.1021/bi00048a003
Date:
08-Nov-95     Release date:   08-Mar-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P23472  (CHLY_HEVBR) -  Hevamine-A
Seq:
Struc: 		311 a.a.
273 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.3.2.1.14  - Chitinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.
   Enzyme class 2: E.C.3.2.1.17  - Lysozyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     vacuole   1 term 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     7 terms  

 

 
DOI no: 10.1021/bi00048a003 Biochemistry 34:15619-15623 (1995)
PubMed id: 7495789  
 
 
Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis.
A.C.Terwisscha van Scheltinga, S.Armand, K.H.Kalk, A.Isogai, B.Henrissat, B.W.Dijkstra.
 
  ABSTRACT  
 
The plant enzyme hevamine has both chitinase and lysozyme activity. HPLC analysis of the products of the hydrolysis of chitopentaose shows that hevamine acts with retention of the configuration, despite the absence of a nucleophilic or stabilizing carboxylate. To analyze the stabilization of a putative oxocarbonium ion intermediate, the X-ray structure of hevamine complexed with the inhibitor allosamidin was determined at 1.85 A resolution. This structure supports the role of Glu127 as a proton donor. The allosamizoline group binds in the center of the active site, mimicking a reaction intermediate in which a positive charge at C1 is stabilized intramolecularly by the carbonyl oxygen of the N-acetyl group at C2.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21299880 E.A.Vasconcelos, C.G.Santana, C.V.Godoy, C.D.Seixas, M.S.Silva, L.R.Moreira, O.B.Oliveira-Neto, D.Price, E.Fitches, E.X.Filho, A.Mehta, J.A.Gatehouse, and M.F.Grossi-De-Sa (2011).
A new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) affects Soybean Asian rust (Phakopsora pachyrhizi) spore germination.
  BMC Biotechnol, 11, 14.  
21240541 T.Ohnuma, T.Numata, T.Osawa, M.Mizuhara, K.M.Vårum, and T.Fukamizo (2011).
Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum.
  Plant Mol Biol, 75, 291-304.
PDB codes: 3alf 3alg
20559485 B.B.Aam, E.B.Heggset, A.L.Norberg, M.Sørlie, K.M.Vårum, and V.G.Eijsink (2010).
Production of chitooligosaccharides and their potential applications in medicine.
  Mar Drugs, 8, 1482-1517.  
20829286 J.Yang, Z.Gan, Z.Lou, N.Tao, Q.Mi, L.Liang, Y.Sun, Y.Guo, X.Huang, C.Zou, Z.Rao, Z.Meng, and K.Q.Zhang (2010).
Crystal structure and mutagenesis analysis of chitinase CrChi1 from the nematophagous fungus Clonostachys rosea in complex with the inhibitor caffeine.
  Microbiology, 156, 3566-3574.
PDB codes: 3g6l 3g6m
20581010 M.Miwa, T.Horimoto, M.Kiyohara, T.Katayama, M.Kitaoka, H.Ashida, and K.Yamamoto (2010).
Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure.
  Glycobiology, 20, 1402-1409.  
19880511 M.Umekawa, C.Li, T.Higashiyama, W.Huang, H.Ashida, K.Yamamoto, and L.X.Wang (2010).
Efficient glycosynthase mutant derived from Mucor hiemalis endo-beta-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan.
  J Biol Chem, 285, 511-521.  
20154467 T.Hirose, T.Sunazuka, and S.Omura (2010).
Recent development of two chitinase inhibitors, Argifin and Argadin, produced by soil microorganisms.
  Proc Jpn Acad Ser B Phys Biol Sci, 86, 85.  
20396401 T.M.Gloster, and D.J.Vocadlo (2010).
Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes.
  Curr Signal Transduct Ther, 5, 74-91.  
20066263 T.M.Gloster, and G.J.Davies (2010).
Glycosidase inhibition: assessing mimicry of the transition state.
  Org Biomol Chem, 8, 305-320.  
19181667 D.W.Abbott, M.S.Macauley, D.J.Vocadlo, and A.B.Boraston (2009).
Streptococcus pneumoniae Endohexosaminidase D, Structural and Mechanistic Insight into Substrate-assisted Catalysis in Family 85 Glycoside Hydrolases.
  J Biol Chem, 284, 11676-11689.
PDB codes: 2w91 2w92
19244232 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.  
19201751 L.Zhang, A.G.Bharadwaj, A.Casper, J.Barkley, J.J.Barycki, and M.A.Simpson (2009).
Hyaluronidase activity of human Hyal1 requires active site acidic and tyrosine residues.
  J Biol Chem, 284, 9433-9442.  
19596709 M.Lienemann, H.Boer, A.Paananen, S.Cottaz, and A.Koivula (2009).
Toward understanding of carbohydrate binding and substrate specificity of a glycosyl hydrolase 18 family (GH-18) chitinase from Trichoderma harzianum.
  Glycobiology, 19, 1116-1126.  
19696236 T.Taira, H.Hayashi, Y.Tajiri, S.Onaga, G.Uechi, H.Iwasaki, T.Ohnuma, and T.Fukamizo (2009).
A plant class V chitinase from a cycad (Cycas revoluta): biochemical characterization, cDNA isolation, and posttranslational modification.
  Glycobiology, 19, 1452-1461.  
19568782 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.  
18975073 Y.Lü, H.Yang, H.Hu, Y.Wang, Z.Rao, and C.Jin (2009).
Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1.
  Glycoconj J, 26, 525-534.  
18323665 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.  
18783954 C.Li, W.Huang, and L.X.Wang (2008).
Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation.
  Bioorg Med Chem, 16, 8366-8372.  
18368288 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.  
18405887 L.X.Wang (2008).
Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation.
  Carbohydr Res, 343, 1509-1522.  
18096701 M.Umekawa, W.Huang, B.Li, K.Fujita, H.Ashida, L.X.Wang, and K.Yamamoto (2008).
Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities.
  J Biol Chem, 283, 4469-4479.  
18587388 S.A.Yuzwa, M.S.Macauley, J.E.Heinonen, X.Shan, R.J.Dennis, Y.He, G.E.Whitworth, K.A.Stubbs, E.J.McEachern, G.J.Davies, and D.J.Vocadlo (2008).
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo.
  Nat Chem Biol, 4, 483-490.
PDB code: 2vvn
17720922 A.P.Bussink, D.Speijer, J.M.Aerts, and R.G.Boot (2007).
Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases.
  Genetics, 177, 959-970.  
17502382 K.E.van Straaten, T.R.Barends, B.W.Dijkstra, and A.M.Thunnissen (2007).
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  J Biol Chem, 282, 21197-21205.
PDB codes: 2pi8 2pic 2pjj
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Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum.
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PDB codes: 2eab 2eac 2ead 2eae
17524989 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: 2uy2 2uy3 2uy4 2uy5
17543889 Zaheer-ul-Haq, P.Dalal, N.N.Aronson, and J.D.Madura (2007).
Family 18 chitolectins: comparison of MGP40 and HUMGP39.
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Screening-based discovery and structural dissection of a novel family 18 chitinase inhibitor.
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PDB code: 2iuz
16704970 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.
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16428844 K.E.Kabir, D.Hirowatari, K.Watanabe, and D.Koga (2006).
Purification and characterization of a novel isozyme of chitinase from Bombyx mori.
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  Proc Natl Acad Sci U S A, 103, 7088-7093.  
16428843 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: 1rd6
16565725 R.J.Dennis, E.J.Taylor, M.S.Macauley, K.A.Stubbs, J.P.Turkenburg, S.J.Hart, G.N.Black, D.J.Vocadlo, and G.J.Davies (2006).
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity.
  Nat Struct Mol Biol, 13, 365-371.
PDB codes: 2chn 2cho
17116887 S.J.Horn, P.Sikorski, J.B.Cederkvist, G.Vaaje-Kolstad, M.Sørlie, B.Synstad, G.Vriend, K.M.Vårum, and V.G.Eijsink (2006).
Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides.
  Proc Natl Acad Sci U S A, 103, 18089-18094.  
16470771 Y.Zeng, J.Wang, B.Li, S.Hauser, H.Li, and L.X.Wang (2006).
Glycopeptide synthesis through endo-glycosidase-catalyzed oligosaccharide transfer of sugar oxazolines: probing substrate structural requirement.
  Chemistry, 12, 3355-3364.  
15795231 M.S.Macauley, G.E.Whitworth, A.W.Debowski, D.Chin, and D.J.Vocadlo (2005).
O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors.
  J Biol Chem, 280, 25313-25322.  
16193156 O.A.Andersen, M.J.Dixon, I.M.Eggleston, and D.M.van Aalten (2005).
Natural product family 18 chitinase inhibitors.
  Nat Prod Rep, 22, 563-579.  
15978043 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.  
14717693 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.  
14597613 G.Vaaje-Kolstad, A.Vasella, M.G.Peter, C.Netter, D.R.Houston, B.Westereng, B.Synstad, V.G.Eijsink, and D.M.van Aalten (2004).
Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.
  J Biol Chem, 279, 3612-3619.
PDB codes: 1ur8 1ur9
15103145 H.Hu, G.Wang, H.Yang, J.Zhou, L.Mo, K.Yang, C.Jin, C.Jin, and Z.Rao (2004).
Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407.
  Acta Crystallogr D Biol Crystallogr, 60, 939-940.  
12890686 B.Aguilera, K.Ghauharali-van der Vlugt, M.T.Helmond, J.M.Out, W.E.Donker-Koopman, J.E.Groener, R.G.Boot, G.H.Renkema, G.A.van der Marel, J.H.van Boom, H.S.Overkleeft, and J.M.Aerts (2003).
Transglycosidase activity of chitotriosidase: improved enzymatic assay for the human macrophage chitinase.
  J Biol Chem, 278, 40911-40916.  
12775711 D.R.Houston, A.D.Recklies, J.C.Krupa, and D.M.van Aalten (2003).
Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes.
  J Biol Chem, 278, 30206-30212.
PDB codes: 1hjv 1hjw 1hjx
12639956 F.V.Rao, D.R.Houston, R.G.Boot, J.M.Aerts, S.Sakuda, and D.M.van Aalten (2003).
Crystal structures of allosamidin derivatives in complex with human macrophage chitinase.
  J Biol Chem, 278, 20110-20116.
PDB codes: 1hki 1hkj 1hkk 1hkm
12728996 K.Suzukawa, T.Yamagami, T.Ohnuma, H.Hirakawa, S.Kuhara, Y.Aso, and M.Ishiguro (2003).
Mutational analysis of amino acid residues involved in catalytic activity of a family 18 chitinase from tulip bulbs.
  Biosci Biotechnol Biochem, 67, 341-346.  
12554965 Y.Papanikolau, G.Tavlas, C.E.Vorgias, and K.Petratos (2003).
De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.
  Acta Crystallogr D Biol Crystallogr, 59, 400-403.
PDB codes: 1edq 1ffq
12092826 B.M.Abdel-Banat, W.Zhou, S.Karasuda, and D.Koga (2002).
Analysis of hydrolytic activity of a 65-kDa chitinase from the silkworm, Bombyx mori.
  Biosci Biotechnol Biochem, 66, 1119-1122.  
  11937059 D.Nurizzo, T.Nagy, H.J.Gilbert, and G.J.Davies (2002).
The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A.
  Structure, 10, 547-556.
PDB codes: 1gqi 1gqj 1gqk 1gql
12093900 D.R.Houston, K.Shiomi, N.Arai, S.Omura, M.G.Peter, A.Turberg, B.Synstad, V.G.Eijsink, and D.M.van Aalten (2002).
High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate.
  Proc Natl Acad Sci U S A, 99, 9127-9132.
PDB codes: 1h0g 1h0i
11846790 E.Bokma, H.J.Rozeboom, M.Sibbald, B.W.Dijkstra, and J.J.Beintema (2002).
Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis.
  Eur J Biochem, 269, 893-901.
PDB codes: 1kqy 1kqz 1kr0 1kr1
11960986 F.Fusetti, H.von Moeller, D.Houston, H.J.Rozeboom, B.W.Dijkstra, R.G.Boot, J.M.Aerts, and D.M.van Aalten (2002).
Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins.
  J Biol Chem, 277, 25537-25544.
PDB codes: 1guv 1lg1 1lg2 1lq0
11821393 P.F.Varela, A.S.Llera, R.A.Mariuzza, and J.Tormo (2002).
Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster.
  J Biol Chem, 277, 13229-13236.
PDB codes: 1jnd 1jne
12171933 S.J.Williams, B.L.Mark, D.J.Vocadlo, M.N.James, and S.G.Withers (2002).
Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state.
  J Biol Chem, 277, 40055-40065.
PDB codes: 1m01 1m03 1m04
11571753 D.Jablonowski, L.Fichtner, V.J.Martin, R.Klassen, F.Meinhardt, M.J.Stark, and R.Schaffrath (2001).
Saccharomyces cerevisiae cell wall chitin, the Kluyveromyces lactis zymocin receptor.
  Yeast, 18, 1285-1299.  
11481469 D.M.van Aalten, D.Komander, B.Synstad, S.Gåseidnes, M.G.Peter, and V.G.Eijsink (2001).
Structural insights into the catalytic mechanism of a family 18 exo-chitinase.
  Proc Natl Acad Sci U S A, 98, 8979-8984.
PDB codes: 1e6n 1e6p 1e6r 1e6z
11327866 T.Fukamizo, C.Sasaki, E.Schelp, K.Bortone, and J.D.Robertus (2001).
Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis.
  Biochemistry, 40, 2448-2454.  
11150614 A.Planas (2000).
Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
  Biochim Biophys Acta, 1543, 361-382.  
11006547 C.S.Rye, and S.G.Withers (2000).
Glycosidase mechanisms.
  Curr Opin Chem Biol, 4, 573-580.  
10823940 D.M.van Aalten, B.Synstad, M.B.Brurberg, E.Hough, B.W.Riise, V.G.Eijsink, and R.K.Wierenga (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.
PDB code: 1e15
10933800 D.O.Hart, S.He, C.J.Chany, S.G.Withers, P.F.Sims, M.L.Sinnott, and H.Brumer (2000).
Identification of Asp-130 as the catalytic nucleophile in the main alpha-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase.
  Biochemistry, 39, 9826-9836.  
10684641 E.J.van Asselt, K.H.Kalk, and B.W.Dijkstra (2000).
Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan.
  Biochemistry, 39, 1924-1934.
PDB codes: 1d0k 1d0l 1d0m
10805791 J.G.Bishop, A.M.Dean, and T.Mitchell-Olds (2000).
Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution.
  Proc Natl Acad Sci U S A, 97, 5322-5327.  
11015121 M.Feix, S.Glöggler, M.Londershausen, W.Weidemann, K.D.Spindler, and M.Spindler-Barth (2000).
A cDNA encoding a chitinase from the epithelial cell line of chironomus tentans (Insecta, diptera) and its functional expression.
  Arch Insect Biochem Physiol, 45, 24-36.  
10771049 R.S.Patil, V.Ghormade, and M.V.Deshpande (2000).
Chitinolytic enzymes: an exploration.
  Enzyme Microb Technol, 26, 473-483.  
10951219 S.Cottaz, B.Brasme, and H.Driguez (2000).
A fluorescence-quenched chitopentaose for the study of endo-chitinases and chitobiosidases.
  Eur J Biochem, 267, 5593-5600.  
  10752616 T.Hollis, A.F.Monzingo, K.Bortone, S.Ernst, R.Cox, and J.D.Robertus (2000).
The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis.
  Protein Sci, 9, 544-551.
PDB code: 1d2k
  10739241 W.Dall'Acqua, and P.Carter (2000).
Substrate-assisted catalysis: molecular basis and biological significance.
  Protein Sci, 9, 1-9.  
  10545329 E.J.van Asselt, A.J.Dijkstra, K.H.Kalk, B.Takacs, W.Keck, and B.W.Dijkstra (1999).
Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand.
  Structure, 7, 1167-1180.
PDB codes: 1qus 1qut
10872458 H.D.Ly, and S.G.Withers (1999).
Mutagenesis of glycosidases.
  Annu Rev Biochem, 68, 487-522.  
10580132 N.O.Keyhani, and S.Roseman (1999).
Physiological aspects of chitin catabolism in marine bacteria.
  Biochim Biophys Acta, 1473, 108-122.  
  10595536 V.Rao, T.Cui, C.Guan, and P.Van Roey (1999).
Mutations of endo-beta-N-acetylglucosaminidase H active site residueAs sp130 anG glu132: activities and conformations.
  Protein Sci, 8, 2338-2346.
PDB codes: 1c3f 1c8x 1c8y 1c90 1c91 1c92 1c93
9539727 K.A.Brameld, and W.A.Goddard (1998).
The role of enzyme distortion in the single displacement mechanism of family 19 chitinases.
  Proc Natl Acad Sci U S A, 95, 4276-4281.  
  9650272 R.Cohen-Kupiec, and I.Chet (1998).
The molecular biology of chitin digestion.
  Curr Opin Biotechnol, 9, 270-277.  
  9385643 G.Pujadas, and J.Palau (1997).
Anatomy of a conformational transition of beta-strand 6 in soybean beta-amylase caused by substrate (or inhibitor) binding to the catalytical site.
  Protein Sci, 6, 2409-2417.  
8673609 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, 638-648.
PDB codes: 1qba 1qbb 1qbc 1qbd
8905079 R.A.Warren (1996).
Microbial hydrolysis of polysaccharides.
  Annu Rev Microbiol, 50, 183-212.  
  8752320 T.Ohno, S.Armand, T.Hata, N.Nikaidou, B.Henrissat, M.Mitsutomi, and T.Watanabe (1996).
A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037.
  J Bacteriol, 178, 5065-5070.  
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