3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase

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For detailed information about serine-type D-Ala-D-Ala carboxypeptidase, go to the full flat file.

Reaction

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

carboxypeptidase I, CPase, D,D-carboxypeptidase, D,D-carboxypeptidase R39, D,D-dipeptidase, D-Ala-D-Ala carboxypeptidase, D-Ala-D-Ala peptidase, D-Ala-D-Ala(D,D) carboxypeptidase, D-alanine carboxypeptidase, D-alanine carboxypeptidase I, D-alanine-carboxypeptidase, D-alanyl carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase/transpeptidase, D-Alanyl-D-alanine hydrolase, D-alanyl-D-alanine peptidase, D-alanyl-D-alanine transpeptidase, D-alanyl-D-alanine-carboxypeptidase, D-alanyl-D-alanine-cleaving peptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanyl-D-alanine-transpeptidase, D-amino acid amidase, DAA, Dac, dacA, DacA-1, DacB, DacC, DacD, DAP, Dbv7, DD-Carboxypeptidase, DD-CPase, DD-CPase1, DD-peptidase, DD-transpeptidase, DD-transpeptidase/penicillin-binding protein, LMM-PBP, low molecular mass penicillin binding protein, PBP, PBP 2, PBP 3, PBP 4, PBP 5, PBP 6, PBP-5*, PBP-6B, PBP1a, PBP1b, PBP2x, PBP3, PBP4, PBP4a, PBP5, PBP6, PBP6a, PBP6b, penicillin binding protein 4, penicillin binding protein 5, penicillin binding proteins, penicillin-binding protein, penicillin-binding protein 1B, penicillin-binding protein 4a, penicillin-binding protein 5, penicillin-binding protein 5a, R39 PBP, SCO4439, serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase, serine-type D-Ala-D-Ala carboxypeptidase, serine-type-D-Ala-D-Ala carboxypeptidase, transpeptidase, VanX, VanXY, VanY, VanY(D) DD-carboxypeptidase, VanYD, VanYn, VC_0947, VP2468, zinc D-Ala-D-Ala carboxypeptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.16 Serine-type carboxypeptidases

                3.4.16.4 serine-type D-Ala-D-Ala carboxypeptidase

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Results	in table
7	Activating Compound
97117	AA Sequence
18	Application
1	CAS Registry Number
27	Cloned(Commentary)
28	Crystallization (Commentary)
15	General Information
2	General Stability
21	IC50 Value
222	Inhibitors
6	kcat/KM [mM/s]
27	Ki Value [mM]
84	KM Value [mM]
53	Localization
6	Metals/Ions
18	Molecular Weight [Da]
53	Natural Substrates/ Products (Substrates)
184	Organism
6	Pathway
323	PDB ID
22	pH Optimum
3	pH Range
27	Protein Variants
32	Purification (Commentary)
3	Reaction
27	Reaction Type
142	Reference
4	Source Tissue
10	Specific Activity [micromol/min/mg]
3	Storage Stability
246	Substrates and Products (Substrate)
13	Subunits
232	Synonyms
13	Temperature Optimum [°C]
5	Temperature Stability [°C]
74	Turnover Number [1/s]

Temperature Stability

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Temperature Stability on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

40

Priestia megaterium

-

inactivation above

36296

49

Escherichia coli

-

melting temperature (Tm), reversible denaturation in a two-state manner. The binding of beta-lactam antibiotics cefoxitin, cloxacillin, moxalactam, and imipenem all stabilize the enzyme significantly with DELTATm values as high as 4.6°C

653782

50

Streptomyces sp.

-

10 min

36307

60

Streptomyces sp.

P39042

half-lives: 120 min for mutant S96A, 220 min for mutant C98A, 30 min for mutant C98N and 170 min for the wild-type enzyme

650206

72

Streptomyces sp.

P39042

half-lives: 3.5 min for mutant K38H, 8 min for mutant S96A, 6 min for mutant C98A, 13 min for mutant enzyme C98A and 10 min for the wild-type enzyme

650206