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Literature summary extracted from

  • 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 (2006), Proc. Natl. Acad. Sci. USA, 103, 8662-8667.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.1.181 medicine enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.181 enzyme shows thioether-linked active site complex with decanoic acid. Structural comparison with lipoate protein ligase A Mycobacterium tuberculosis
6.3.1.20 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 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.181 Mycobacterium tuberculosis P9WK83 enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
-
2.3.1.181 Mycobacterium tuberculosis H37Rv P9WK83 enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
-
6.3.1.20 Mycobacterium tuberculosis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.181 octanoyl-[acyl-carrier protein] + protein = protein 6-N-(octanoyl)lysine + acyl carrier protein enzyme functions as a cysteine/lysine dyad acyltransferase, where K142 and C176 are acid/base catalysts. Reaction proceeds via an internal thioester intermediate Mycobacterium tuberculosis
a

Synonyms

EC Number Synonyms Comment Organism
2.3.1.181 LipB
-
 Mycobacterium tuberculosis