Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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C.Goedl,
and
B.Nidetzky
(2009).
Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate.
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Chembiochem, 10,
2333-2337.
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J.R.Rich,
and
S.G.Withers
(2009).
Emerging methods for the production of homogeneous human glycoproteins.
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Nat Chem Biol, 5,
206-215.
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K.J.Loft,
P.Bojarová,
K.Slámová,
V.Kren,
and
S.J.Williams
(2009).
Synthesis of sulfated glucosaminides for profiling substrate specificities of sulfatases and fungal beta-N-acetylhexosaminidases.
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Chembiochem, 10,
565-576.
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M.D.Balcewich,
K.A.Stubbs,
Y.He,
T.W.James,
G.J.Davies,
D.J.Vocadlo,
and
B.L.Mark
(2009).
Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ.
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Protein Sci, 18,
1541-1551.
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PDB codes:
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A.Scaffidi,
K.A.Stubbs,
R.J.Dennis,
E.J.Taylor,
G.J.Davies,
D.J.Vocadlo,
and
R.V.Stick
(2007).
A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of beta-N-acetylglucosaminidases.
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Org Biomol Chem, 5,
3013-3019.
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PDB code:
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J.D.Funkhouser,
and
N.N.Aronson
(2007).
Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family.
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BMC Evol Biol, 7,
96.
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R.Ettrich,
V.Kopecký,
K.Hofbauerová,
V.Baumruk,
P.Novák,
P.Pompach,
P.Man,
O.Plíhal,
M.Kutý,
N.Kulik,
J.Sklenár,
H.Ryslavá,
V.Kren,
and
K.Bezouska
(2007).
Structure of the dimeric N-glycosylated form of fungal beta-N-acetylhexosaminidase revealed by computer modeling, vibrational spectroscopy, and biochemical studies.
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BMC Struct Biol, 7,
32.
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S.G.Manuel,
C.Ragunath,
H.B.Sait,
E.A.Izano,
J.B.Kaplan,
and
N.Ramasubbu
(2007).
Role of active-site residues of dispersin B, a biofilm-releasing beta-hexosaminidase from a periodontal pathogen, in substrate hydrolysis.
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FEBS J, 274,
5987-5999.
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C.Mayer,
D.J.Vocadlo,
M.Mah,
K.Rupitz,
D.Stoll,
R.A.Warren,
and
S.G.Withers
(2006).
Characterization of a beta-N-acetylhexosaminidase and a beta-N-acetylglucosaminidase/beta-glucosidase from Cellulomonas fimi.
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FEBS J, 273,
2929-2941.
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K.A.Stubbs,
N.Zhang,
and
D.J.Vocadlo
(2006).
A divergent synthesis of 2-acyl derivatives of PUGNAc yields selective inhibitors of O-GlcNAcase.
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Org Biomol Chem, 4,
839-845.
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M.Wacker,
M.F.Feldman,
N.Callewaert,
M.Kowarik,
B.R.Clarke,
N.L.Pohl,
M.Hernandez,
E.D.Vines,
M.A.Valvano,
C.Whitfield,
and
M.Aebi
(2006).
Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems.
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Proc Natl Acad Sci U S A, 103,
7088-7093.
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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.
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Nat Struct Mol Biol, 13,
365-371.
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PDB codes:
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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.
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Chemistry, 12,
3355-3364.
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A.Sørbotten,
S.J.Horn,
V.G.Eijsink,
and
K.M.Vårum
(2005).
Degradation of chitosans with chitinase B from Serratia marcescens. Production of chito-oligosaccharides and insight into enzyme processivity.
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FEBS J, 272,
538-549.
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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.
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Eur J Biochem, 271,
253-262.
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C.W.Reid,
N.T.Blackburn,
and
A.J.Clarke
(2004).
The effect of NAG-thiazoline on morphology and surface hydrophobicity of Escherichia coli.
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FEMS Microbiol Lett, 234,
343-348.
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H.Dvir,
M.Harel,
A.A.McCarthy,
L.Toker,
I.Silman,
A.H.Futerman,
and
J.L.Sussman
(2003).
X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease.
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EMBO Rep, 4,
704-709.
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PDB code:
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J.B.Kaplan,
C.Ragunath,
N.Ramasubbu,
and
D.H.Fine
(2003).
Detachment of Actinobacillus actinomycetemcomitans biofilm cells by an endogenous beta-hexosaminidase activity.
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J Bacteriol, 185,
4693-4698.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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499 a.a.
_CL
-hexosaminidase. A, detailed SpHEX catalytic mechanism. The general acid/base (Glu314) and the residue (Asp313) primarily responsible for stabilizing positive charge on the oxazolinium ion intermediate are shown, although no attempt is made to indicate their true locations. Hydroxyl groups and C6 have been removed from the pyranose ring for clarity. B, chemical structure of the cyclic intermediate analogue NAG-thiazoline.
1 and +1 of SpHEX, respectively. Semi-transparent surfaces have been drawn around hydrophobic residues using GRASP (50). The catalytic triad (Glu314, His250, and Asp191) has been drawn along with its hydrogen-bonding network. The glycerol hydroxyl group hydrogen bonding to the carboxylate of Glu314 is believed to occupy the position that an incoming water molecule would take to nucleophilically attack C-1. WAT indicates the conserved incoming water molecule proposed by Ref. 10.
