D-alanyl-D-alanine carboxypeptidase
Details
- Name
- D-alanyl-D-alanine carboxypeptidase
- Synonyms
- 3.4.16.4
- DD-carboxypeptidase
- Gene Name
- Not Available
- Organism
- Streptomyces sp. (strain R61)
- Amino acid sequence
>lcl|BSEQ0010942|D-alanyl-D-alanine carboxypeptidase MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVR VDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNT YLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGV TNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTH ANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQ QWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNV NVLNTMARTLESAFCGKPTTAKLRSATSSATTVERHEDIAPGIARD
- Number of residues
- 406
- Molecular Weight
- 42916.725
- Theoretical pI
- 6.03
- GO Classification
- Functionsserine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall organization / peptidoglycan biosynthetic process / regulation of cell shapeComponentsextracellular region
- General Function
- Serine-type d-ala-d-ala carboxypeptidase activity
- Specific Function
- Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).
- Pfam Domain Function
- Beta-lactamase (PF00144)
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0002678|1221 bp ATGGTCTCAGGAACGGTGGGCAGAGGTACGGCGCTGGGCGCGGTGCTGTTGGCCCTCCTC GCAGTCCCCGCACAGGCCGGCACCGCCGCGGCCGCGGATCTGCCGGCACCCGACGACACC GGTCTGCAGGCGGTGCTGCACACGGCCCTTTCCCAGGGAGCCCCCGGTGCGATGGTGCGG GTCGACGACAACGGCACGATCCACCAGTTGTCGGAGGGAGTCGCCGACCGGGCCACCGGG CGTGCGATCACCACGACCGACCGGTTCCGCGTCGGCAGCGTCACCAAGAGCTTCTCCGCC GTGGTCCTGCTGCAACTGGTGGACGAGGGCAAGCTCGACCTGGACGCTTCGGTGAACACC TATCTGCCCGGGCTGCTGCCCGACGACCGGATCACCGTGCGTCAGGTGATGAGCCACCGC AGTGGGCTGTACGACTACACCAACGACATGTTCGCGCAGACGGTCCCGGGCTTCGAGTCC GTCCGCAACAAGGTCTTCAGCTACCAGGACCTGATCACCCTGTCCCTCAAGCACGGGGTC ACCAACGCACCGGGCGCGGCCTATTCATACTCCAACACGAACTTCGTCGTCGCGGGCATG CTCATCGAGAAGCTCACCGGCCACTCCGTGGCCACGGAGTACCAGAACCGCATCTTCACG CCGCTGAACCTGACCGACACCTTCTACGTGCACCCCGACACCGTCATCCCGGGCACCCAC GCCAACGGCTACCTCACGCCGGACGAGGCCGGTGGGGCCCTGGTCGACTCCACCGAGCAG ACGGTGTCGTGGGCGCAGAGCGCGGGCGCGGTCATCTCCAGCACGCAGGACCTGGACACG TTCTTCTCCGCGTTGATGAGCGGGCAGCTCATGTCCGCCGCGCAGCTCGCGCAGATGCAG CAGTGGACGACGGTCAACAGCACCCAGGGGTACGGCCTCGGCCTGCGCCGCCGTGACCTG TCCTGCGGTATCTCGGTGTACGGCCACACGGGCACCGTGCAGGGCTACTACACGTACGCC TTCGCCTCGAAGGACGGCAAGCGCAGCGTCACCGCGCTCGCCAACACCTCGAACAACGTG AACGTGCTGAACACGATGGCCCGCACGCTGGAATCCGCGTTCTGCGGCAAGCCGACGACC GCGAAGCTGCGCAGCGCGACCTCCTCGGCGACCACCGTGGAGCGCCACGAGGACATCGCG CCGGGTATCGCCCGCGACTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P15555 UniProtKB Entry Name DAC_STRSR GenBank Protein ID 515050 GenBank Gene ID X05109 - General References
- Duez C, Piron-Fraipont C, Joris B, Dusart J, Urdea MS, Martial JA, Frere JM, Ghuysen JM: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur J Biochem. 1987 Feb 2;162(3):509-18. [Article]
- Duez C, Piron-Fraipont C, Joris B, Dusart J, Urdea MS, Martial JA, Frere JM, Ghuysen JM: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur J Biochem. 1994 Sep 15;224(3):1079. [Article]
- Joris B, Jacques P, Frere JM, Ghuysen JM, Van Beeumen J: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data. Eur J Biochem. 1987 Feb 2;162(3):519-24. [Article]
- Piron-Fraipont C, Lenzini MV, Dusart J, Ghuysen JM: Transcriptional analysis of the DD-peptidase/penicillin-binding protein-encoding dac gene of Streptomyces R61: use of the promoter and signal sequences in a secretion vector. Mol Gen Genet. 1990 Aug;223(1):114-20. [Article]
- Knox JR, Pratt RF: Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein. Antimicrob Agents Chemother. 1990 Jul;34(7):1342-7. [Article]
- Kelly JA, Knox JR, Moews PC, Hite GJ, Bartolone JB, Zhao H, Joris B, Frere JM, Ghuysen JM: 2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams. J Biol Chem. 1985 May 25;260(10):6449-58. [Article]
- Kelly JA, Kuzin AP: The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution. J Mol Biol. 1995 Nov 24;254(2):223-36. [Article]
- McDonough MA, Anderson JW, Silvaggi NR, Pratt RF, Knox JR, Kelly JA: Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins. J Mol Biol. 2002 Sep 6;322(1):111-22. [Article]
- Silvaggi NR, Anderson JW, Brinsmade SR, Pratt RF, Kelly JA: The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state. Biochemistry. 2003 Feb 11;42(5):1199-208. [Article]
- Silvaggi NR, Josephine HR, Kuzin AP, Nagarajan R, Pratt RF, Kelly JA: Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin". J Mol Biol. 2005 Jan 21;345(3):521-33. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01786 D-Alanine experimental unknown Details DB01868 Glycyl-L-a-Aminopimelyl-E-(D-2-Aminoethyl)Phosphonate experimental unknown Details DB02136 Cephalosporin analog experimental unknown Details DB02514 (2Z)-3-{[Oxido(oxo)phosphoranyl]oxy}-2-phenylacrylate experimental unknown Details DB02578 N-[(6S)-6-Carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine experimental unknown Details DB00456 Cefalotin approved, investigational, vet_approved yes inhibitor Details DB03313 Cephalosporin C experimental unknown Details DB03820 (2S,5R,6R)-6-({(6S)-6-[(Ammonioacetyl)amino]-6-carboxylatohexanoyl}amino)-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate experimental unknown Details DB03843 Formaldehyde approved, vet_approved unknown Details DB03927 Glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine experimental unknown Details DB04340 2-[(Dioxidophosphoranyl)oxy]benzoate experimental unknown Details DB04488 (6S)-N-[(2S,3R,6R,7R)-3-(Acetyloxymethyl)-2-carboxy-8-oxo-5-thia-1-azabicyclo[4.2.0]octan-7-yl]-6-[(2-aminoacetyl)amino]-7-hydroxy-7-oxoheptanimidate experimental unknown Details DB03450 Cephalothin Group experimental unknown Details