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MetaCyc Reaction: 6.2.1.42

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 6.2.1.42

Enzymes and Genes:

Mycobacterium tuberculosis : 3-oxocholest-4-en-26-oate--CoA ligase Inferred from experiment : fadD19
Rhodococcus rhodochrous : 3-oxocholest-4-en-26-oate–CoA ligase Inferred from experiment : fadD19
Saccharomyces cerevisiae : acyl-CoA synthetase : FAA2

In Pathway: cholesterol degradation to androstenedione II (cholesterol dehydrogenase) , cholesterol degradation to androstenedione I (cholesterol oxidase)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: 3-oxocholest-4-en-26-oate–CoA ligase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -12.71167 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyses a step in the degradation of cholesterol. It is responsible for the activation of the C8 side chain. 3β-hydroxycholest-5-en-26-oate can also be used as substrate.

Citations: [Casabon14, Wilbrink11]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a long-chain fatty acid + ATP + coenzyme A → a long-chain acyl-CoA + AMP + diphosphate] (6.2.1.3):
i1: palmitate + ATP + coenzyme A → palmitoyl-CoA + AMP + diphosphate (6.2.1.3)

Instance reactions of [a 2,3,4-saturated fatty acid + ATP + coenzyme A → a 2,3,4-saturated fatty acyl CoA + AMP + diphosphate] (6.2.1.3):
i2: pristanate + ATP + coenzyme A → pristanoyl-CoA + AMP + diphosphate (6.2.1.3)

i3: phytanate + ATP + coenzyme A → phytanoyl-CoA + AMP + diphosphate (6.2.1.24)

i4: hexanoate + ATP + coenzyme A → hexanoyl-CoA + AMP + diphosphate (6.2.1.-)

i5: decanoate + ATP + coenzyme A → decanoyl-CoA + AMP + diphosphate (6.2.1.3)

i6: octanoate + ATP + coenzyme A → octanoyl-CoA + AMP + diphosphate (6.2.1.3)

i7: a 2-methyl branched 2,3,4-saturated fatty acid + ATP + coenzyme A → a 2-methyl branched 2,3,4-saturated fatty acyl-CoA + AMP + diphosphate (6.2.1.3)

i8: a 3-methyl-branched 2,3,4-saturated fatty acid + ATP + coenzyme A → a 3-methyl-branched 2,3,4-saturated fatty acyl-CoA + AMP + diphosphate (6.2.1.3)

i9: an odd numbered straight chain 2,3,4-saturated fatty acid + ATP + coenzyme A → an odd numbered straight chain 2,3,4-saturated fatty acyl CoA + AMP + diphosphate (6.2.1.3)

i10: a (R)-2-hydroxy even numbered straight chain 2,3,4-saturated fatty acid + ATP + coenzyme A → a (R)-2-hydroxy even numbered straight chain 2,3,4-saturated fatty acyl CoA + AMP + diphosphate (6.2.1.-)

Relationship Links: BRENDA:EC:6.2.1.42 , ENZYME:EC:6.2.1.42 , IUBMB-ExplorEnz:EC:6.2.1.42

Credits:
Created 04-Oct-2011 by Caspi R , SRI International


References

Casabon14: Casabon I, Swain K, Crowe AM, Eltis LD, Mohn WW (2014). "Actinobacterial acyl coenzyme a synthetases involved in steroid side-chain catabolism." J Bacteriol 196(3);579-87. PMID: 24244004

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Wilbrink11: Wilbrink MH, Petrusma M, Dijkhuizen L, van der Geize R (2011). "FadD19 of Rhodococcus rhodochrous DSM43269, a steroid-coenzyme A ligase essential for degradation of C-24 branched sterol side chains." Appl Environ Microbiol 77(13);4455-64. PMID: 21602385


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed May 27, 2015, BIOCYC13B.