N(2)-(2-carboxyethyl)arginine synthase

Details

Name
N(2)-(2-carboxyethyl)arginine synthase
Synonyms
  • 2.5.1.66
  • CEA synthetase
Gene Name
ceaS
Organism
Streptomyces clavuligerus
Amino acid sequence
>lcl|BSEQ0019401|N(2)-(2-carboxyethyl)arginine synthase
MSRVSTAPSGKPTAAHALLSRLRDHGVGKVFGVVGREAASILFDEVEGIDFVLTRHEFTA
GVAADVLARITGRPQACWATLGPGMTNLSTGIATSVLDRSPVIALAAQSESHDIFPNDTH
QCLDSVAIVAPMSKYAVELQRPHEITDLVDSAVNAAMTEPVGPSFISLPVDLLGSSEGID
TTVPNPPANTPAKPVGVVADGWQKAADQAAALLAEAKHPVLVVGAAAIRSGAVPAIRALA
ERLNIPVITTYIAKGVLPVGHELNYGAVTGYMDGILNFPALQTMFAPVDLVLTVGYDYAE
DLRPSMWQKGIEKKTVRISPTVNPIPRVYRPDVDVVTDVLAFVEHFETATASFGAKQRHD
IEPLRARIAEFLADPETYEDGMRVHQVIDSMNTVMEEAAEPGEGTIVSDIGFFRHYGVLF
ARADQPFGFLTSAGCSSFGYGIPAAIGAQMARPDQPTFLIAGDGGFHSNSSDLETIARLN
LPIVTVVVNNDTNGLIELYQNIGHHRSHDPAVKFGGVDFVALAEANGVDATRATNREELL
AALRKGAELGRPFLIEVPVNYDFQPGGFGALSI
Number of residues
573
Molecular Weight
60906.59
Theoretical pI
4.85
GO Classification
Functions
magnesium ion binding / N2-(2-carboxyethyl)arginine synthase activity / thiamine pyrophosphate binding
General Function
Thiamine pyrophosphate binding
Specific Function
Involved in the biosynthesis of the beta-lactamase inhibitor, clavulanic acid. Catalyzes the thiamine diphosphate (ThDP) dependent condensation of D-glyceraldehyde-3-phosphate (D-G3P) with L-arginine to yield the beta-amino acid, N2-(2-carboxyethyl)arginine (CEA) via a beta-elimination resulting in the formation of an enol which undergoes a second elimination to generate the alpha,beta-unsaturated acryloyl-ThDP.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0006386|1722 bp
ATGTCCCGTGTATCGACCGCCCCCAGCGGCAAGCCTACCGCCGCTCACGCCCTCCTGTCA
CGGTTGCGTGATCACGGTGTGGGGAAGGTGTTTGGGGTTGTCGGCCGAGAGGCCGCGTCG
ATTCTCTTCGACGAGGTCGAGGGGATCGACTTCGTTCTGACCCGCCACGAGTTCACCGCG
GGTGTCGCCGCTGATGTCCTCGCGCGGATCACCGGTCGCCCCCAGGCGTGCTGGGCCACC
CTGGGCCCCGGTATGACCAACCTCTCCACCGGTATCGCCACGTCCGTCCTGGACCGCTCG
CCGGTCATCGCGCTCGCCGCGCAGTCGGAGTCGCACGACATCTTCCCGAACGACACCCAC
CAGTGCCTGGACTCGGTGGCGATCGTCGCCCCGATGTCCAAGTACGCCGTGGAGCTCCAG
CGGCCCCACGAGATCACCGACCTCGTCGACTCCGCCGTGAACGCGGCCATGACCGAGCCG
GTCGGGCCCTCCTTCATCTCCCTCCCGGTGGACCTGCTCGGCTCCTCCGAGGGCATCGAC
ACCACCGTCCCCAACCCGCCGGCGAACACCCCGGCGAAACCGGTCGGCGTCGTCGCCGAC
GGCTGGCAGAAGGCCGCCGACCAGGCCGCCGCCCTGCTCGCCGAGGCCAAGCACCCGGTG
CTCGTCGTCGGAGCGGCCGCGATCCGCTCGGGCGCCGTCCCGGCGATCCGCGCCCTGGCC
GAGCGCCTGAACATCCCGGTCATCACGACCTACATCGCCAAGGGTGTCCTGCCGGTCGGC
CACGAGCTGAACTACGGCGCCGTCACCGGCTACATGGACGGCATCCTCAACTTCCCGGCG
CTCCAGACCATGTTCGCCCCGGTGGACCTCGTCCTCACCGTCGGCTACGACTACGCCGAG
GACCTGCGCCCGTCCATGTGGCAGAAGGGCATCGAGAAGAAGACCGTCCGTATCTCCCCG
ACGGTCAACCCGATCCCCCGGGTCTACCGGCCCGACGTCGACGTCGTCACCGACGTCCTC
GCCTTCGTGGAGCACTTCGAGACCGCGACCGCCTCCTTCGGGGCCAAGCAGCGCCACGAC
ATCGAGCCGCTGCGCGCCCGGATCGCGGAGTTCCTGGCCGACCCGGAGACCTACGAGGAC
GGCATGCGCGTCCACCAGGTCATCGACTCCATGAACACCGTCATGGAGGAGGCCGCCGAG
CCCGGCGAGGGCACGATCGTCTCCGACATCGGCTTCTTCCGTCACTACGGTGTGCTCTTC
GCCCGCGCCGACCAGCCCTTCGGCTTCCTCACCTCGGCGGGCTGCTCCAGCTTCGGCTAC
GGCATCCCCGCCGCCATCGGCGCCCAGATGGCCCGCCCGGACCAGCCGACCTTCCTCATC
GCGGGTGACGGCGGCTTCCACTCCAACAGCTCCGACCTGGAGACCATCGCCCGGCTCAAC
CTGCCGATCGTGACCGTCGTCGTCAACAACGACACCAACGGCCTGATCGAGCTGTACCAG
AACATCGGTCACCACCGCAGCCACGACCCGGCGGTCAAGTTCGGCGGCGTCGACTTCGTC
GCGCTCGCCGAGGCCAACGGTGTCGACGCCACCCGCGCCACCAACCGCGAGGAGCTGCTC
GCGGCCCTGCGCAAGGGTGCCGAGCTGGGTCGTCCGTTCCTCATCGAGGTCCCGGTCAAC
TACGACTTCCAGCCGGGCGGCTTCGGCGCCCTGAGCATCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9LCV9
UniProtKB Entry NameCEAS_STRCL
GenBank Gene IDU87786
General References
  1. Aidoo KA, Wong A, Alexander DC, Rittammer RA, Jensen SE: Cloning, sequencing and disruption of a gene from Streptomyces clavuligerus involved in clavulanic acid biosynthesis. Gene. 1994 Sep 15;147(1):41-6. [Article]
  2. Paradkar AS, Aidoo KA, Wong A, Jensen SE: Molecular analysis of a beta-lactam resistance gene encoded within the cephamycin gene cluster of Streptomyces clavuligerus. J Bacteriol. 1996 Nov;178(21):6266-74. [Article]
  3. Paradkar AS, Aidoo KA, Jensen SE: A pathway-specific transcriptional activator regulates late steps of clavulanic acid biosynthesis in Streptomyces clavuligerus. Mol Microbiol. 1998 Feb;27(4):831-43. [Article]
  4. Jensen SE, Elder KJ, Aidoo KA, Paradkar AS: Enzymes catalyzing the early steps of clavulanic acid biosynthesis are encoded by two sets of paralogous genes in Streptomyces clavuligerus. Antimicrob Agents Chemother. 2000 Mar;44(3):720-6. [Article]
  5. Merski M, Townsend CA: Observation of an acryloyl-thiamin diphosphate adduct in the first step of clavulanic acid biosynthesis. J Am Chem Soc. 2007 Dec 26;129(51):15750-1. Epub 2007 Dec 5. [Article]
  6. Caines ME, Elkins JM, Hewitson KS, Schofield CJ: Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway. J Biol Chem. 2004 Feb 13;279(7):5685-92. Epub 2003 Nov 17. [Article]
  7. Caines ME, Sorensen JL, Schofield CJ: Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase. Biochem Biophys Res Commun. 2009 Aug 7;385(4):512-7. doi: 10.1016/j.bbrc.2009.05.095. Epub 2009 May 27. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01987Cocarboxylaseapproved, experimentalunknownDetails