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
Functions
serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall organization / peptidoglycan biosynthetic process / regulation of cell shape
Components
extracellular 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
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
ResourceLink
UniProtKB IDP15555
UniProtKB Entry NameDAC_STRSR
GenBank Protein ID515050
GenBank Gene IDX05109
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01786D-AlanineexperimentalunknownDetails
DB01868Glycyl-L-a-Aminopimelyl-E-(D-2-Aminoethyl)PhosphonateexperimentalunknownDetails
DB02136Cephalosporin analogexperimentalunknownDetails
DB02514(2Z)-3-{[Oxido(oxo)phosphoranyl]oxy}-2-phenylacrylateexperimentalunknownDetails
DB02578N-[(6S)-6-Carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanineexperimentalunknownDetails
DB00456Cefalotinapproved, investigational, vet_approvedyesinhibitorDetails
DB03313Cephalosporin CexperimentalunknownDetails
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-carboxylateexperimentalunknownDetails
DB03843Formaldehydeapproved, vet_approvedunknownDetails
DB03927Glycyl-L-alpha-amino-epsilon-pimelyl-D-alanineexperimentalunknownDetails
DB043402-[(Dioxidophosphoranyl)oxy]benzoateexperimentalunknownDetails
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-oxoheptanimidateexperimentalunknownDetails
DB03450Cephalothin GroupexperimentalunknownDetails