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EC 2.7.7.63 Details
EC number
2.7.7.63
Accepted name
lipoate—protein ligase
Reaction
(1) ATP + lipoate = diphosphate + lipoyl-AMP;;(2) lipoyl-AMP + apoprotein = protein N6-(lipoyl)lysine + AMP
Other name(s)
LplA, lipoate protein ligase, lipoate-protein ligase A, LPL, LPL-B
Systematic name
ATP:lipoate adenylyltransferase
CAS registry number
144114-18-1
Comment
Requires Mg2+. Both 6S- and 6R-lipoates can act as substrates but there is a preference for the naturally occurring R-form. Selenolipoate, i.e. 5-(1,2-diselenolan-3-yl)pentanoic acid, and 6-sulfanyloctanoate can also act as substrates, but more slowly [2]. This enzyme is responsible for lipoylation in the presence of exogenous lipoic acid [7]. Lipoylation is essential for the function of several 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]. This enzyme attaches lipoic acid to the lipoyl domains of these proteins, converting apoproteins into holoproteins. It is likely that an alternative pathway, involving EC 2.3.1.181, lipoyl(octanoyl) transferase and EC 2.8.1.8, lipoyl synthase, is the normal route for lipoylation [7].
History
created 2006, deleted 2016
EC Tree
1.12.7.1 created 1972, deleted 1978
2.7.7.16 created 1961, deleted 1972, [transferred to EC 3.1.4.22, deleted 1980]
2.7.7.17 created 1965, deleted 1972, [transferred to EC 3.1.4.23, deleted 1980]
2.7.7.20 created 1965, deleted 1972
2.7.7.26 created 1961 as EC 3.1.4.8, transferred 1965 to EC 2.7.7.26, deleted 1972
2.7.7.29 created 1972, deleted 2004