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EC Tree
IUBMB Comments Not identical with EC 6.2.1.20 long-chain-fatty-acid---[acyl-carrier-protein] ligase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
Phytanoyl-CoA ligase, Phytanoyl-CoA synthetase, Synthetase, phytanoyl coenzyme A,
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Phytanoyl-CoA ligase
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Phytanoyl-CoA synthetase
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Synthetase, phytanoyl coenzyme A
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ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA
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Acid-thiol ligation
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phytanate:CoA ligase (AMP-forming)
Not identical with EC 6.2.1.20 long-chain-fatty-acid---[acyl-carrier-protein] ligase.
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ATP + phytanate + CoA
AMP + diphosphate + phytanoyl-CoA
CTP + phytanate + CoA
CMP + diphosphate + phytanoyl-CoA
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low activity compared to ATP
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-
?
GTP + phytanate + CoA
GMP + diphosphate + phytanoyl-CoA
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low activity compared to ATP
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-
?
ITP + phytanate + CoA
IMP + diphosphate + phytanoyl-CoA
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low activity compared to ATP
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-
?
UTP + phytanate + CoA
UMP + diphosphate + phytanoyl-CoA
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low activity compared to ATP
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-
?
ATP + phytanate + CoA
?
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activation of phytanic acid to phytanoyl-CoA is prerequisite for its alpha-oxidation
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?
ATP + phytanate + CoA
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phytanoyl-CoA ligase in peroxisomal membrane regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes
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?
ATP + phytanate + CoA
AMP + diphosphate + phytanoyl-CoA
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?
ATP + phytanate + CoA
AMP + diphosphate + phytanoyl-CoA
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?
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ATP + phytanate + CoA
?
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activation of phytanic acid to phytanoyl-CoA is prerequisite for its alpha-oxidation
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?
ATP + phytanate + CoA
?
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phytanoyl-CoA ligase in peroxisomal membrane regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes
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?
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Mg2+
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absolutely required, optimal concentration: 60 mM, inhibition at high concentrations
Mn2+
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can replace Mg2+ at 5 mM, inhibition at high concentrations
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AMP
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11 mM, 50% inhibition
iodoacetic acid
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75 mM, 100% inhibition
NEM
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10 mM, 87% inhibition
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brenda
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brenda
enzyme is different from long chain acyl-CoA ligase, EC 6.2.1.3
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brenda
rat liver long-chain acyl-CoA synthetase activity and phytanoyl-CoA synthetase activity are catalyzed by one enzyme protein
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brenda
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skin, cell culture
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the enzyme is synthesized on the cytoplasmic surface and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes
brenda
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ACSL1_CAVPO
698
1
77698
Swiss-Prot
other Location (Reliability: 2 )
ACSL1_HUMAN
698
1
77943
Swiss-Prot
other Location (Reliability: 4 )
ACSL1_MOUSE
699
1
77951
Swiss-Prot
other Location (Reliability: 2 )
ACSL1_RAT
699
1
78179
Swiss-Prot
other Location (Reliability: 2 )
S27A2_HUMAN
620
3
70312
Swiss-Prot
Secretory Pathway (Reliability: 1 )
S27A2_MOUSE
620
2
70423
Swiss-Prot
Secretory Pathway (Reliability: 1 )
S27A2_RAT
620
2
70694
Swiss-Prot
Secretory Pathway (Reliability: 1 )
A1KA13_AZOSB
Azoarcus sp. (strain BH72)
532
0
57633
TrEMBL
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Muralidharan, F.N.; Muralidharan, V.B.
Phytanoyl-CoA ligase activity in rat liver
Biochem. Int.
13
123-130
1986
Rattus norvegicus
brenda
Pahan, K.; Singh, I.
Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes
J. Lipid Res.
36
986-997
1995
Homo sapiens
brenda
Pahan, K.; Gulati, S.; Singh, I.
Phytanic acid alpha-oxidation in rat liver mitochondria
Biochim. Biophys. Acta
1201
491-497
1994
Rattus norvegicus
brenda
Pahan, K.; Cofer, J.; Baliga, P.; Singh, I.
Identification of phytanoyl-CoA ligase as a distinct acyl-CoA ligase in peroxisomes from cultured skin fibroblasts
FEBS Lett.
322
101-104
1993
Homo sapiens
brenda
Watkins, P.A.; Howard, A.E.; Gould, S.J.; Avigan, J.; Mihalik, S.J.
Phytanic acid activation in rat liver peroxisomes is catalyzed by long-chain acyl-CoA synthetase
J. Lipid Res.
37
2288-2295
1996
Rattus norvegicus
brenda
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Transporter Classification Database (TCDB):
4.C.1.1.5
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6.2.1.24 phytanate-CoA ligase
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