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| Enzyme Name | | UniProtKB | KEGG |
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| P00733 |
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| Protein name | Zinc D-Ala-D-Ala carboxypeptidase | zinc D-Ala-D-Ala carboxypeptidaseZn2+ G peptidase, D-alanyl-D-alanine hydrolaseD-alanyl-D-alanine-cleaving carboxypeptidaseDD-carboxypeptidaseG enzymeDD-carboxypeptidase-transpeptidase |
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| Synonyms | EC 3.4.17.14D-alanyl-D-alanine carboxypeptidaseMetallo DD-peptidaseZn DD-peptidase |
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| MEROPS | M15.001 (Metallo)
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| Pfam | PF08291 (Peptidase_M15_3)
PF01471 (PG_binding_1)
[Graphical view]
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| UniProtKB:Accession Number | P00733 |
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| Entry name | CBPM_STRAL |
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| Activity | Cleavage of the bond: (Ac)(2)-L-lysyl-D- alanyl-|-D-alanine. |
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| Subunit |
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| Subcellular location | Secreted. |
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| Cofactor | Binds 1 zinc ion per subunit. |
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| Active-site residues | | resource |
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| Swiss-prot;P00733 & literature [3], [9] | | pdb | Catalytic residues | Cofactor-binding residues |
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| | | | | | | | | | |
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| 1lbuA01 |  |  |  |  |  |  |  |
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| 1lbuA02 | | | | | | | | TYR 189;HIS 192;ASP 194;HIS 195
| HIS 154;ASP 161;HIS 197(Zinc binding)
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| References for Catalytic Mechanism | | References | Sections | No. of steps in catalysis |
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| [3] | p.470 |
| | [8] | Fig.1, p.77-78 |
| | [9] | Fig.8, p.172-174 |
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| references | | [1] |
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| PubMed ID | 7409166 |
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| Journal | FEBS Lett |
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| Year | 1980 |
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| Volume | 117 |
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| Pages | 212-4 |
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| Authors | Dideberg O, Charlier P, Dupont L, Vermeire M, Frere JM, Ghuysen JM |
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| Title | The 4.5 A resolution structure analysis of the exocellular DD-carboxypeptidase of Streptomyces albus G. |
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| [2] |
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| Journal | FEBS LETTERS |
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| Year | 1980 |
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| Volume | 117 |
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| Pages | 215-218 |
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| Authors | O. Dideberga, B. Jorisb, J. M. Frereb, J. M. Ghuysenb, G. Weberc, R. Robayec, J. M. Delbrouckc and I. Roelandtsd |
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| Title | The exocellular DD-carboxypeptidase of Streptomyces albus G: A metallo (Zn2+) enzyme |
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| [3] |
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| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
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| Medline ID | 83012968 |
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| PubMed ID | 7121588 |
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| Journal | Nature |
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| Year | 1982 |
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| Volume | 299 |
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| Pages | 469-70 |
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| Authors | Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM |
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| Title | Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution. |
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| Related UniProtKB | P00733 |
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| [4] |
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| PubMed ID | 7123246 |
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| Journal | Science |
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| Year | 1982 |
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| Volume | 218 |
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| Pages | 479-81 |
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| Authors | Kelly JA, Moews PC, Knox JR, Frere JM, Ghuysen JM |
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| Title | Penicillin target enzyme and the antibiotic binding site. |
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| [5] |
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| PubMed ID | 6743245 |
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| Journal | Biochem J |
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| Year | 1984 |
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| Volume | 219 |
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| Pages | 763-72 |
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| Authors | Charlier P, Dideberg O, Jamoulle JC, Frere JM, Ghuysen JM, Dive G, Lamotte-Brasseur J |
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| Title | Active-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G. |
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| [6] |
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| PubMed ID | 11848831 |
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| Journal | Chem Rev |
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| Year | 1996 |
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| Volume | 96 |
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| Pages | 2375-2434 |
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| Authors | Lipscomb WN, Strater N |
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| Title | Recent Advances in Zinc Enzymology. |
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| [7] |
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| PubMed ID | 9614972 |
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| Journal | Cell Mol Life Sci |
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| Year | 1998 |
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| Volume | 54 |
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| Pages | 353-8 |
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| Authors | Kelly JA, Kuzin AP, Charlier P, Fonze E |
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| Title | X-ray studies of enzymes that interact with penicillins. |
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| [8] |
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| PubMed ID | 9702193 |
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| Journal | Mol Cell |
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| Year | 1998 |
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| Volume | 2 |
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| Pages | 75-84 |
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| Authors | Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH |
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| Title | The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. |
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| [9] |
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| Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
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| Journal | Handbook of Metalloproteins |
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| Year | 2004 |
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| Volume | 3 |
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| Pages | 164-175 |
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| Authors | Charlier, P., Wery, J.-P., Dideberg, O., Frere, J.-M |
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| Title | Streptomyces Albus G D-Ala-A-Ala Carboxypeptidase |
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| Related PDB | 1lbu |
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| Related UniProtKB | P00733 |
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| comments | This enzyme belongs to the peptidase M15 family.
According to the literature [8] & [9], the reaction proceeds as follows:
(1) The carbonyl oxygen of substrate peptide bond is bound to zinc ion, whereas the catalytic water bound to the zinc is slightly shifted to His195.
(2) Asp194 modulates the activity of His195.
(3) His195 acts as a general base, to activate the catalytic water along with the zinc ion.
(4) The activated water makes a nucleophilic attack on the carbonyl carbon of the substrate, leading to the formation of tetrahedral oxyanion intermediate.
(5) The negative charge on the intermediate is stabilized by the sidechains of His192 and Tyr189 together with the zinc ion.
(6) His195 now acts as a general acid, to protonate the leaving amine group through a water.
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| created | updated |
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| 2004-04-27 | 2009-02-26 |
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