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Information on EC 6.3.1.20 - lipoate-protein ligase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WK83

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IUBMB Comments
Requires Mg2+. This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid . The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) . Lipoylation is essential for the function of these enzymes. The enzyme can also use octanoate instead of lipoate.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WK83
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipoic acid ligase, lipoate protein ligase, lpla1, lipoate-protein ligase, lipoate ligase, lipoate-protein ligase a, lipoyl ligase, lipoic acid protein ligase, lipl1, oslpla, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoate protein ligase B
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
[lipoyl-carrier protein]-L-lysine:lipoate ligase (AMP-forming)
Requires Mg2+. This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid [7]. The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [6]. Lipoylation is essential for the function of these enzymes. The enzyme can also use octanoate instead of lipoate.
CAS REGISTRY NUMBER
COMMENTARY hide
139639-26-2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NSC164080
i.e. methyl 2-(2-(((benzyloxy)carbonyl)amino)propanamido)-3-(4-hydroxyphenyl)propanoate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structural comparison of lipoate-protein ligase with cysteine/lysine dyad acyltransferase LipB shows conserved structural and sequence active-site features, but 4’-phosphopantheine-bound octanoic acid recognition is a specific property of cysteine/lysine dyad acyltransferase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, Q.; Zhao, X.; Nasser Eddine, A.; Geerlof, A.; Li, X.; Cronan, J.E.; Kaufmann, S.H.; Wilmanns, M.
The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase
Proc. Natl. Acad. Sci. USA
103
8662-8667
2006
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Billones, J.; Carrillo, M.; Organo, V.; MacAlino, S.; Emnacen, I.; Sy, J.
Virtual screening against Mycobacterium tuberculosis lipoate protein ligase B (MtbLipB) and in Silico ADMET evaluation of top hits
Orient. J. Chem.
29
1457-1468
2013
Mycobacterium tuberculosis (P9WK83), Mycobacterium tuberculosis ATCC 25618 (P9WK83)
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Manually annotated by BRENDA team