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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1cdg

E.C. namecyclomaltodextrin glucanotransferase
SpeciesBacillus circulans (Bacteria)
E.C. Number (IntEnz) 2.4.1.19
CSA Homologues of 1cdgThere are 159 Homologs
CSA Entries With UniProtID P43379
CSA Entries With EC Number 2.4.1.19
PDBe Entry 1cdg
PDBSum Entry 1cdg
MACiE Entry M0045

Literature Report

Introduction
Mechansim

Catalytic Sites for 1cdg

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA328macie:sideChainIts negatively charged side chain also stabilises the oxocarbenium transition states.
GluA257macie:sideChainIt acts as a base protonates the glycosidic oxygen of the scissile bond in the first step and then deprotonates the attacking hydroxyl group in the second step.
AspA229macie:sideChainIt acts as a nucleophile to attack the sugar, forming the covalent linkage within the intermediate. Its carboxylate group carbonyl oxygen also stabilises the transition state.
ArgA227254macie:sideChain
HisA327354macie:sideChain

Literature References

Notes:
Lawson CL
Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form.
J Mol Biol 1994 236 590-600
PubMed: 8107143
Uitdehaag JC
X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family.
Nat Struct Biol 1999 6 432-436
PubMed: 10331869
Knegtel RM
Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
J Biol Chem 1995 270 29256-29264
PubMed: 7493956
Mosi R
Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme.
Biochemistry 1997 36 9927-9934
PubMed: 9245426
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