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Details on Person ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA

Class:Id	Reaction:389889
_displayName	ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA
_doRelease	TRUE
_timestamp	2024-06-19 22:22:14
authored	[InstanceEdit:398115] D'Eustachio, P, 2009-03-16 18:50:14
catalystActivity	[CatalystActivity:389900] pristanoyl-CoA oxidase activity of ACOX2:FAD, ACOXL:FAD [peroxisomal matrix]
catalystActivityReference	[CatalystActivityReference:9914047] pristanoyl-CoA oxidase activity of ACOX2:FAD, ACOXL:FAD [peroxisomal matrix] The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney
compartment	[Compartment:17951] peroxisomal matrix
created	[InstanceEdit:389895] D'Eustachio, P, 2009-01-19 22:23:09
crossReference	[DatabaseIdentifier:9914026] RHEA:40460
edited	[InstanceEdit:398202] D'Eustachio, P, 2009-03-18 13:33:40
input	[SimpleEntity:389893] (2S) Pristanoyl-CoA [peroxisomal matrix] [SimpleEntity:113535] O2 [peroxisomal matrix]
literatureReference	[LiteratureReference:193409] The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney [LiteratureReference:192346] Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome
modified	[InstanceEdit:392189] D'Eustachio, P, 2009-02-27 15:24:50 [InstanceEdit:398114] D'Eustachio, P, 2009-03-16 18:51:20 [InstanceEdit:398263] Matthews, L, 2009-03-18 17:59:11 [InstanceEdit:8848537] Jassal, Bijay, 2015-12-09 [InstanceEdit:8848538] Jassal, Bijay, 2015-12-09 [InstanceEdit:8848540] Jassal, Bijay, 2015-12-09 [InstanceEdit:9830342] Matthews, Lisa, 2023-03-08 [InstanceEdit:9914019] D'Eustachio, Peter, 2024-06-19
name	ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA (2S)-pristanoyl-CoA + O2 => (2E)-pristenoyl-CoA + H2O2 (2S)-pristanoyl-CoA + O2 => trans-2,3-dehydropristanoyl-CoA + H2O2 (ACOX2)
output	[SimpleEntity:389894] trans-2,3-dehydropristanoyl-CoA [peroxisomal matrix] [SimpleEntity:113575] H2O2 [peroxisomal matrix]
precedingEvent	[Reaction:389897] Isomerization of (2R)-pristanoyl-CoA to (2S)-pristanoyl-CoA [Homo sapiens] [Reaction:389632] pristanate + CoA-SH + ATP => pristanoyl-CoA + AMP + pyrophosphate [Homo sapiens]
releaseDate	2009-04-01
releaseStatus	UPDATED
reviewed	[InstanceEdit:392190] Jassal, Bijay, 2009-02-27
reviewStatus	[ReviewStatus:9821382] five stars
revised	[InstanceEdit:8848539] Jassal, Bijay, 2015-12-09
species	[Species:48887] Homo sapiens
stableIdentifier	[StableIdentifier:398443] R-HSA-389889.4
summation	[Summation:389885] In human liver and kidney tissue, monomeric peroxisomal ACOX...
(hasEvent)	[Pathway:389887] Beta-oxidation of pristanoyl-CoA [Homo sapiens]
(precedingEvent)	[Reaction:389986] trans-2,3-dehydropristanoyl-CoA + H2O => 3-hydroxypristanoyl-CoA [Homo sapiens]
(updatedInstance)	[_UpdateTracker:9783616] Update Tracker - [Reaction:389889] ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA - v56:[modifyText]
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No pathways have been reviewed or authored by ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA (389889)