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Information on EC 2.3.1.204 - octanoyl-[GcvH]:protein N-octanoyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P39648

for references in articles please use BRENDA:EC2.3.1.204
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IUBMB Comments
In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
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Bacillus subtilis
UNIPROT: P39648
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
LIPL, octanoyl-[GcvH]:E2 amidotransferase, ywfL, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octanoyl-[GcvH]:E2 amidotransferase
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PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase
In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
show the reaction diagram
-
-
-
r
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
show the reaction diagram
-
-
-
r
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
show the reaction diagram
-
the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31420
calculated from amino acid sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, N.; Christensen, Q.H.; Mansilla, M.C.; Cronan, J.E.; de Mendoza, D.
A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
Mol. Microbiol.
80
335-349
2011
Bacillus subtilis (P39648)
Manually annotated by BRENDA team
Christensen, Q.H.; Martin, N.; Mansilla, M.C.; de Mendoza, D.; Cronan, J.E.
A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
Mol. Microbiol.
80
350-363
2011
Bacillus subtilis (P39648), Bacillus subtilis 168 (P39648)
Manually annotated by BRENDA team
Rasetto, N.B.; Lavatelli, A.; Martin, N.; Mansilla, M.C.
Unravelling the lipoyl-relay of exogenous lipoate utilization in Bacillus subtilis
Mol. Microbiol.
112
302-316
2019
Bacillus subtilis, Bacillus subtilis JH642
Manually annotated by BRENDA team