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Information on EC 6.2.1.24 - phytanate-CoA ligase

for references in articles please use BRENDA:EC6.2.1.24

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EC Tree

6 Ligases

6.2 Forming carbon-sulfur bonds

6.2.1 Acid-thiol ligases

6.2.1.24 phytanate-CoA ligase

IUBMB Comments

Not identical with EC 6.2.1.20 long-chain-fatty-acid---[acyl-carrier-protein] ligase.

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6.2.1.24
phytanic
alpha-oxidation
acyl-coa
peroxisomes
pristanic
refsum
ligases
palmitoyl-coa
palmitic
lignoceric
manuscript
beta-oxidation
rhizomelic
branched-chain
chondrodysplasia
punctata
5,8,11,14-eicosatetraynoic

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

Reaction Schemes

Synonyms

phytanoyl-coa ligase, phytanoyl-coa synthetase, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Phytanoyl-CoA ligase

Phytanoyl-CoA synthetase

Synthetase, phytanoyl coenzyme A

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA

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REACTION TYPE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Acid-thiol ligation

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SYSTEMATIC NAME

IUBMB Comments

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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CAS REGISTRY NUMBER

COMMENTARY

105238-50-4

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

ATP + phytanate + CoA

2 entries

ATP + phytanate + CoA

AMP + diphosphate + phytanoyl-CoA

2 entries

CTP + phytanate + CoA

CMP + diphosphate + phytanoyl-CoA

Rattus norvegicus

low activity compared to ATP

702

GTP + phytanate + CoA

GMP + diphosphate + phytanoyl-CoA

Rattus norvegicus

low activity compared to ATP

702

ITP + phytanate + CoA

IMP + diphosphate + phytanoyl-CoA

Rattus norvegicus

low activity compared to ATP

702

UTP + phytanate + CoA

UMP + diphosphate + phytanoyl-CoA

Rattus norvegicus

low activity compared to ATP

702

ATP + phytanate + CoA

Homo sapiens

activation of phytanic acid to phytanoyl-CoA is prerequisite for its alpha-oxidation

705

ATP + phytanate + CoA

Homo sapiens

phytanoyl-CoA ligase in peroxisomal membrane regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes

703

ATP + phytanate + CoA

AMP + diphosphate + phytanoyl-CoA

Homo sapiens

703, 705

ATP + phytanate + CoA

AMP + diphosphate + phytanoyl-CoA

Rattus norvegicus

702, 704

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ATP + phytanate + CoA

2 entries

ATP + phytanate + CoA

Homo sapiens

activation of phytanic acid to phytanoyl-CoA is prerequisite for its alpha-oxidation

705

ATP + phytanate + CoA

Homo sapiens

phytanoyl-CoA ligase in peroxisomal membrane regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes

703

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mg2+

Rattus norvegicus

absolutely required, optimal concentration: 60 mM, inhibition at high concentrations

702

Mn2+

Rattus norvegicus

can replace Mg2+ at 5 mM, inhibition at high concentrations

702

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

AMP

Rattus norvegicus

11 mM, 50% inhibition

702

iodoacetic acid

Rattus norvegicus

75 mM, 100% inhibition

702

NEM

Rattus norvegicus

10 mM, 87% inhibition

702

palmitic acid

Rattus norvegicus

702

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0286

phytanic acid

Rattus norvegicus

702

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

AMP

Rattus norvegicus

702

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

8.7

Rattus norvegicus

Tris-HCl buffer

702

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Homo sapiens

703, 705

brenda

Rattus norvegicus

3 entries

Rattus norvegicus

704

brenda

Rattus norvegicus

enzyme is different from long chain acyl-CoA ligase, EC 6.2.1.3

702

brenda

Rattus norvegicus

rat liver long-chain acyl-CoA synthetase activity and phytanoyl-CoA synthetase activity are catalyzed by one enzyme protein

706

brenda

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

adipose tissue

Rattus norvegicus

702

brenda

fibroblast

Homo sapiens

skin, cell culture

705

brenda

heart

Rattus norvegicus

702

brenda

kidney

Rattus norvegicus

702

brenda

703

brenda

liver

Rattus norvegicus

702, 704

brenda

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

endoplasmic reticulum

Homo sapiens

5783

705

brenda

microsome

Rattus norvegicus

702

brenda

705

brenda

mitochondrion

Rattus norvegicus

5739

702, 704

brenda

peroxisome

Homo sapiens

5777

705

brenda

peroxisome

Homo sapiens

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

5777

703

brenda

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

Q9JID6 pBLAST

ACSL1_CAVPO

Cavia porcellus

698

77698

Swiss-Prot

Show Sequence

other Location (Reliability: 2)

P33121 pBLAST

ACSL1_HUMAN

Homo sapiens

698

77943

Swiss-Prot

Show Sequence

other Location (Reliability: 4)

P41216 pBLAST

ACSL1_MOUSE

Mus musculus

699

77951

Swiss-Prot

Show Sequence

other Location (Reliability: 2)

P18163 pBLAST

ACSL1_RAT

Rattus norvegicus

699

78179

Swiss-Prot

Show Sequence

other Location (Reliability: 2)

O14975 pBLAST

S27A2_HUMAN

Homo sapiens

620

70312

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 1)

O35488 pBLAST

S27A2_MOUSE

Mus musculus

620

70423

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 1)

P97524 pBLAST

S27A2_RAT

Rattus norvegicus

620

70694

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 1)

A1KA13 pBLAST

A1KA13_AZOSB

Azoarcus sp. (strain BH72)

532

57633

TrEMBL

Show Sequence

other Location (Reliability: 2)

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Rattus norvegicus

t1/2: 3-5 min

702

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

702

Muralidharan, F.N.; Muralidharan, V.B.

Phytanoyl-CoA ligase activity in rat liver

Biochem. Int.

123-130

1986

Rattus norvegicus

3753503

brenda

703

Pahan, K.; Singh, I.

Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes

J. Lipid Res.

986-997

1995

Homo sapiens

7544821

brenda

704

Pahan, K.; Gulati, S.; Singh, I.

Phytanic acid alpha-oxidation in rat liver mitochondria

Biochim. Biophys. Acta

1201

491-497

1994

Rattus norvegicus

7803482

brenda

705

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

8482375

brenda

706

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.

2288-2295

1996

Rattus norvegicus

8978480

brenda

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EXTERNAL LINKS (specific for EC-Number 6.2.1.24)

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

IUBMB Enzyme Nomenclature

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)

Transporter Classification Database (TCDB): 4.C.1.1.5

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