EzCatDB: S00407
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DB codeS00407
RLCP classification1.13.11110.262 : Hydrolysis
CATH domainDomain 13.40.630.10 : AminopeptidaseCatalytic domain
E.C.3.4.17.18

CATH domainRelated DB codes (homologues)
3.40.630.10 : AminopeptidaseD00512,S00406,D00192,D00193,D00467

Enzyme Name
UniProtKBKEGG

P29068
Protein nameCarboxypeptidase Tcarboxypeptidase T
CPT
SynonymsEC 3.4.17.18
MEROPSM14.007 (Metallo)
PfamPF00246 (Peptidase_M14)
[Graphical view]


UniProtKB:Accession NumberP29068
Entry nameCBPT_THEVU
ActivityReleases a C-terminal residue, which may be hydrophobic or positively charged.
SubunitMonomer.
Subcellular location
CofactorBinds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00017C00012C00001C00017C00012C00045
CompoundZincProteinPeptideH2OProteinPeptideAmino acid
Typeheavy metalpeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/proteinamino acids
ChEBI29105


15377



PubChem32051


962
22247451



               
1obrABound:_ZNUnboundUnboundBound:HOH 9UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P29068 & literature [1],[2]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1obrAARG 129;GLU 277
HIS 69;GLU 72;HIS 204(Zinc binding)
THR 205

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.284-286

references
[1]
CommentsX-ray crystallography (2.35 Angstroms)
Medline ID92394121
PubMed ID1521526
JournalEur J Biochem
Year1992
Volume208
Pages281-8
AuthorsTeplyakov A, Polyakov K, Obmolova G, Strokopytov B, Kuranova I, Osterman A, Grishin N, Smulevitch S, Zagnitko O, Galperina O, et al
TitleCrystal structure of carboxypeptidase T from Thermoactinomyces vulgaris.
Related PDB1obr
Related UniProtKBP29068
[2]
PubMed ID1449602
JournalJ Protein Chem
Year1992
Volume11
Pages561-70
AuthorsOsterman AL, Grishin NV, Smulevitch SV, Matz MV, Zagnitko OP, Revina LP, Stepanov VM
TitlePrimary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family.

comments
This enzyme belongs to the peptidase family-M14.
This enzyme binds four calcium ions which seem to play an important role in the thermostability of the enzyme, according to the Swiss-prot data (P29068).
Moreover, this enzyme is homologous to carboxypeptidase A (E.C. 3.4.17.1; D00467 in EzCatDB), carboxypeptidase A2 (E.C. 3.4.17.15; D00193) and carboxypeptidase B (E.C. 3.4.17.2; D00512) with conserved catalytic residues. Thus, they might have the same catalytic mechanism.
According to the literature [1], the zinc-bound water molecule could be considered as a possible nucleophile, whilst Arg129 is believed to polarize the carbonyl of the scissile bond of the substrate as the stabilizer of the 'oxyanion hole'.
The paper [2] also characterized the catalytic residues as follows:
(1) Glu277 (of 1obr) promotes nucleophilic attack of H2O molecule on substrate carbonyl and subsequent proton transfer in general base mechanism.
(2) His69, Glu72 and His204 (of 1obr) are ligated to the zinc ion that is presumed to take part in H2O polarization and the stabilization of the tetrahedral intermediate.
(3) Arg129 (1obr) plays an essential role in stabilizing the tetrahedral intermediate.

createdupdated
2002-09-272009-02-26


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