BRENDA - Reference to 2.3.1.181; Id = 737308

Saccharomyces cerevisiae

-

additional information

Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2

737308

Saccharomyces cerevisiae

?

-

octanoyl-CoA + [glycine cleavage system 3]-L-lysine

-

737308

Saccharomyces cerevisiae

[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA

-

?

octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine

-

737308

Saccharomyces cerevisiae

[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA

-

?

octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine

-

737308

Saccharomyces cerevisiae

[pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA

-

?

octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine

-

737308

Saccharomyces cerevisiae

[glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein

in vitro reaction

-

?

additional information

Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2

737308

Saccharomyces cerevisiae

?

-

octanoyl-CoA + [glycine cleavage system 3]-L-lysine

-

737308

Saccharomyces cerevisiae

[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA

-

?

octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine

-

737308

Saccharomyces cerevisiae

[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA

-

?

octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine

-

737308

Saccharomyces cerevisiae

[pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA

-

?

octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine

-

737308

Saccharomyces cerevisiae

[glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein

in vitro reaction

-

?

physiological function

octanoyltransferase Lip2 specifically modifies glycine cleavage system 3 using octanoyl-ACP from mitochondrial FA biosynthesis. When all glycine cleavage system 3 is octanoylated, octanoyl-ACP accumulates. An octanoyl-ACP: CoA transferase transfers the octanoyl moiety to CoA, providing substrate for octanoyltransferase Lip3 to modify pyruvate dehydrogenase and oxoglutarate dehydrogenase. Complementation of the Escherichia coli DELTAlipB DELTAlplA strain by expression of Lip3 requires a host-encoded acyl-CoA synthase

Saccharomyces cerevisiae

physiological function

octanoyltransferase Lip2 specifically modifies glycine cleavage system 3 using octanoyl-ACP from mitochondrial FA biosynthesis. When all glycine cleavage system 3 is octanoylated, octanoyl-ACP accumulates. An octanoyl-ACP: CoA transferase transfers the octanoyl moiety to CoA, providing substrate for octanoyltransferase Lip3 to modify pyruvate dehydrogenase and oxoglutarate dehydrogenase. Complementation of the Escherichia coli DELTAlipB DELTAlplA strain by expression of Lip3 requires a host-encoded acyl-CoA synthase

Saccharomyces cerevisiae

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Two redundant octanoyltransfer ...

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Lipoate-protein ligase and oct ...

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Hermes

The role of the Saccharomyces ...

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A novel amidotransferase requi ...

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Lipoic acid synthesis: a new f ...

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Scavenging of cytosolic octano ...

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6796-6803

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Knockout studies reveal an imp ...

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PLoS ONE

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Crystal structure of bovine li ...

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The Mycobacterium tuberculosis ...

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661184

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The reaction of LipB, the octa ...

Escherichia coli

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663308

Nesbitt

Expression, purification, and ...

Escherichia coli

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The Escherichia coli lipB gene ...

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663062

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Lipoic acid metabolism in Arab ...

Arabidopsis thaliana

Plant Cell Physiol.

42

650-656

2001

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662098

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A new metabolic link. The acyl ...

Escherichia coli, Neurospora crassa, Pisum sativum

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17903-17906

1997

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2

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661982

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Lipoic acid metabolism in Esch ...

Escherichia coli

J. Bacteriol.

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6411-6420

1991

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The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis

Data extracted from this reference: