| Name | aminopeptidase |
|---|---|
| Synonyms | Aminopeptidase; PGCP; Plasma glutamate carboxypeptidase; Plasma glutamate carboxypeptidases |
| Name | DMPA |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 10673442 | Bompard-Gilles C, Villeret V, Davies GJ, Fanuel L, Joris B, Frere JM, Van Beeumen J: A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi. Structure. 2000 Feb 15;8(2):153-62. BACKGROUND: The L-aminopeptidase D--esterase/amidase from Ochrobactrum anthropi (DmpA) releases the N-terminal L and/or D- residues from peptide substrates. |
32(0,1,1,2) | Details |
| 15937278 | Cheng H, Grishin NV: DOM-fold: a structure with crossing loops found in DmpA, acetyltransferase, and -binding domain. Protein Sci. 2005 Jul;14(7):1902-10. Epub 2005 Jun 3. Here, we define a novel DOM-fold as a consensus structure of the domains in DmpA (L-aminopeptidase D--esterase/amidase), OAT acetyltransferase), and MocoBD -binding domain), and discuss possible evolutionary scenarios of its origin. |
31(0,1,1,1) | Details |
| 15955066 | Komeda H, Asano Y: A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for beta-alanyl dipeptides. FEBS J. 2005 Jun;272(12):3075-84. MCI3434 genome and found an additional gene, bapA, coding for a protein showing sequence similarity to DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 (43% identity). |
12(0,0,2,2) | Details |
| 10089474 | Bompard-Gilles C, Villeret V, Fanuel L, Joris B, Frere JM, Van Beeumen J: Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):699-701. Ochrobactrum anthropi possesses an L-aminopeptidase (DmpA) also able to act as a D-amidase/D-esterase. |
7(0,0,1,2) | Details |
| 10377256 | Fanuel L, Goffin C, Cheggour A, Devreese B, Van Driessche G, Joris B, Van Beeumen J, Frere JM: The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family. Biochem J. 1999 Jul 1;341 ( Pt 1):147-55. |
7(0,0,1,2) | Details |
| 15352873 | Elkins JM, Kershaw NJ, Schofield CJ: X-ray crystal structure of acetyltransferase from the clavulanic acid biosynthesis gene cluster. Biochem J. 2005 Jan 15;385(Pt 2):565-73. However, differences in the connectivity reveal that OATs belong to a structural family different from that of other structurally characterized Ntn enzymes, with one exception: unexpectedly, the alphabetabetaalpha sandwich of ORF6 (where ORF stands for open reading frame) displays the same fold as an DmpA (L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi), and so the OATs and DmpA form a new structural subfamily of Ntn enzymes. |
6(0,0,1,1) | Details |
| 17193247 | Heck T, Limbach M, Geueke B, Zacharias M, Gardiner J, Kohler HP, Seebach D: Enzymatic degradation of beta- and mixed alpha,beta-oligopeptides. Chem Biodivers. 2006 Dec;3(12):1325-48. In this work, the L-aminopeptidase-D-amidase/esterase (DmpA) from Ochrobactrum anthropi LMG7991 is compared to two closely related beta-peptidyl aminopeptidases (BapA), which originate from Sphingosinicella strains, and to microsomal leucine aminopeptidase (LAP) as a reference. |
6(0,0,1,1) | Details |
| 20340152 | Heck T, Reimer A, Seebach D, Gardiner J, Deniau G, Lukaszuk A, Kohler HP, Geueke B: beta-Aminopeptidase-Catalyzed Biotransformations of beta (2)-Dipeptides: Kinetic Resolution and Enzymatic Coupling. Chembiochem. 2010 Mar 25. We have previously shown that the beta-aminopeptidases BapA from Sphingosinicella xenopeptidilytica and DmpA from Ochrobactrum anthropi can catalyze reactions with non-natural beta (3)-peptides and beta (3)-amino acid amides. |
1(0,0,0,1) | Details |
| 10379365 | Fanuel L, Thamm I, Kostanjevecki V, Samyn B, Joris B, Goffin C, Brannigan J, Van Beeumen J, Frere JM: Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide. Cell Mol Life Sci. 1999 May;55(5):812-8. The second enzyme, DmpA, exhibits a similar substrate profile when tested on p-nitroanilide derivatives of and L/D- but the amounts produced by the Ochrobactrum strain were not sufficient to allow complete purification. |
0(0,0,0,0) | Details |