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Catalytic Site Atlas

CSA LITERATURE entry for 1cz1

E.C. nameglucan 1,3-beta-glucosidase
SpeciesCandida albicans (Yeast)
E.C. Number (IntEnz)
CSA Homologues of 1cz1There are 20 Homologs
CSA Entries With UniProtID P29717
CSA Entries With EC Number
PDBe Entry 1cz1
PDBSum Entry 1cz1
MACiE Entry 1cz1

Literature Report

IntroductionFungal exo-beta-(1,3)-glucanases, such as that from the human pathogen Candida albicans, belong to the glycosyl hydrolase family 5 that also includes many bacterial cellulases. The C. albicans enzyme is involved in the metabolism of cell wall glucan. It catalyses the hydrolytic removal of glucose residues from the non-reducing end of beta-1,3-glucan and (to a lesser extent) beta-1,6-glucan, the two main structural components of the C. albicans cell wall. The enzyme also has glucosyl transferase activity in which a molecule other than water can accept the removed glucose residue. This may be important in shaping the cell wall during morphogenesis.
MechansimThe reaction proceeds by a double displacement mechanism with net retention of configuration at the anomeric C1 position. Nucleophilic attack by Glu 292 leads to displacement of the leaving group and formation of a covalent glucosyl-enzyme intermediate via a presumed oxo-carbenium ion-like transition state. Glu 192 acts as a general acid to protonate the departing leaving group.

Catalytic Sites for 1cz1

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA192230macie:sideChainActs as a general acid to protonate the leaving group in formation of the glycosyl-enzyme intermediate. Later acts as a general base to abstract a proton from water so that it can carry out a nucleophilic attack on the the intermediate.
GluA292330macie:sideChainAttacks the glycosidic bond to form a glycosyl-enzyme intermediate via a presumed oxo-carbenium ion-like transition state.

Literature References

Notes:Residues Glu 192 and Glu 292 may also be referred to in the literature as Glu 230 and Glu 330 respectively, if the preprotein is used to define the amino acid ordering.
Mackenzie LF
Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase.
J Biol Chem 1997 272 3161-3167
PubMed: 9013549
Cutfield SM
The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases.
J Mol Biol 1999 294 771-783
PubMed: 10610795
Chambers RS
Identification of a putative active site residue in the exo-beta-(1,3)-glucanase of Candida albicans.
FEBS Lett 1993 327 366-369
PubMed: 8348966