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Information on EC 6.3.2.8 - UDP-N-acetylmuramate-L-alanine ligase and Organism(s) Haemophilus influenzae and UniProt Accession P45066

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IUBMB Comments
Involved in the synthesis of a cell-wall peptide in bacteria.
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This record set is specific for:
Haemophilus influenzae
UNIPROT: P45066
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The taxonomic range for the selected organisms is: Haemophilus influenzae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
udp-n-acetylmuramate:l-alanine ligase, murc ligase, udp-n-acetylmuramate-l-alanine ligase, udp-n-acetylmuramoyl:l-alanine ligase, udp-n-acetylmuramic acid l-alanine ligase, udp-n-acetylmuramoyl-l-alanine synthetase, udp-n-acetylmuramyl:l-alanine ligase, udp-murnac:l-alanine ligase, l-alanine adding enzyme, uridine diphosphate n-acetylmuramate:l-alanine ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Alanine-adding enzyme
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L-Ala ligase
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L-Alanine adding enzyme
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Synthetase, uridine diphospho-N-acetylmuramoylalanine
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UDP-acetylmuramoyl-L-alanine synthetase
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UDP-MurNAc:L-alanine ligase
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UDP-N-acetylmuramate-alanine ligase
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UDP-N-acetylmuramoyl-L-alanine synthetase
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UDP-N-acetylmuramoylalanine synthetase
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UDP-N-acetylmuramyl:L-alanine ligase
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Uridine 5´-diphosphate-N-acetylmuramyl-L-alanine synthetase
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Uridine diphosphate N-acetylmuramate:L-alanine ligase
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Uridine diphospho-N-acetylmuramoylalanine synthetase
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Uridine-diphosphate-N-acetylmuramate:L-alanine ligase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
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carboxamide formation
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)
Involved in the synthesis of a cell-wall peptide in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-52-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of active fully assembled substrate- and product-bound complexes. Selenomethionine-substituted enzyme preparations used for structure determination. Crystals obtained by drop vapor diffusion experiments
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified with ProBond nickel-chelating resin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mol, C.D.; Brooun, A.; Dougan, D.R.; Hilgers, M.T.; Tari, L.W.; Wijnands, R.A.; Knuth, M.W.; McRee, D.E.; Swanson, R.V.
Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae
J. Bacteriol.
185
4152-4162
2003
Haemophilus influenzae (P45066)
Manually annotated by BRENDA team