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Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase

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UNIPROT: Q9LCC8 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
Synonyms
transpeptidase, penicillin-binding protein, pbp2x, pbp1a, pbp1b, penicillin binding proteins, pbp 2, pbp 3, pbp 5, dd-peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-amino acid amidase
lacks peptidase activity
carboxypeptidase I
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-
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CPase
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-
-
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D-alanine carboxypeptidase
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D-alanine carboxypeptidase I
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-
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D-alanyl carboxypeptidase
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-
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D-alanyl-D-alanine carboxypeptidase
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-
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D-Alanyl-D-alanine hydrolase
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-
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D-alanyl-D-alanine peptidase
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-
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D-alanyl-D-alanine-carboxypeptidase
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-
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D-alanyl-D-alanine-cleaving peptidase
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-
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D-alanyl-D-alanine-cleaving-peptidase
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DD-Carboxypeptidase
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DD-peptidase
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DD-transpeptidase
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-
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PBP-5*
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PBP-6B
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-
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PBP5
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penicillin binding protein 5
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VanX
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VanY
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
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PATHWAY SOURCE
PATHWAYS
-
-, -, -
CAS REGISTRY NUMBER
COMMENTARY hide
9077-67-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-amino acid amide + H2O
D-amino acid + ammonia
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-amino acid amide + H2O
D-amino acid + ammonia
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ochrobactrum anthropi SV3
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9LCC8_BRUAN
363
0
40082
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structures of native D-amino acid amidase and of the D-phenylalanine/D-amino acid amidase complex are determined at 2.1 and at 2.4 A resolution, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the pET15b vector for expression in Escherichia coli cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okazaki, S.; Suzuki, A.; Komeda, H.; Yamaguchi, S.; Asano, Y.; Yamane, T.
Crystal structure and functional characterization of a D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3, a new member of the penicillin-recognizing proteins
J. Mol. Biol.
368
79-91
2007
Brucella anthropi (Q9LCC8), Brucella anthropi
Manually annotated by BRENDA team