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Information on EC 5.1.99.4 - alpha-methylacyl-CoA racemase and Organism(s) Rattus norvegicus and UniProt Accession P70473

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     5 Isomerases
         5.1 Racemases and epimerases
             5.1.99 Acting on other compounds
                5.1.99.4 alpha-methylacyl-CoA racemase
IUBMB Comments
alpha-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates. Also active towards some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Not active towards free acids
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Rattus norvegicus
UNIPROT: P70473
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
amacr, p504s, alpha-methylacyl-coa racemase, alpha-methylacyl-coenzyme a racemase, alpha-methylacyl coenzyme a racemase, alpha-methylacyl coa racemase, amacr/p504s, 2-methylacyl-coa racemase, alpha-methyl coa racemase, 2-arylpropionyl-coa epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-arylpropionyl-CoA epimerase
-
-
-
-
2-methylacyl-CoA racemase
-
-
-
-
alpha-Methylacyl CoA racemase
-
-
-
-
alpha-methylacyl-CoA racemase
-
-
GenBank U89905-derived protein GI2145184
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-
-
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GenBank U89906-derived protein GI 2145186
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-
-
-
Racemase, alpha-methylacyl coenzyme A
-
-
-
-
Racemase, alpha-methylacyl coenzyme A (Mus musculus clone 3)
-
-
-
-
Racemase, alpha-methylacyl coenzyme A (Rattus norvegicus clone 11)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
2-Methylacyl-CoA 2-epimerase
alpha-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates. Also active towards some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Not active towards free acids
CAS REGISTRY NUMBER
COMMENTARY hide
156681-44-6
-
197731-71-8
racemase, alpha-methylacyl coenzyme A (Mus musculus clone 3) /genBank U89906-derived protein GI 2145186
197731-72-9
racemase, alpha-methylacyl coenzyme A (Rattus norvegicus clone 11) /genBank U89905-derived protein GI2145184
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(25S)-trihydroxycoprostanoyl-CoA
(25R)-trihydroxycoprostanoyl-CoA
show the reaction diagram
-
-
-
-
?
(2S)-2-methylacyl-CoA
(2R)-2-methylacyl-CoA
show the reaction diagram
(2S)-pristanoyl-CoA
(2R)-pristanoyl-CoA
show the reaction diagram
-
-
-
-
?
(S)-2-Methylmyristoyl-CoA
(R)-2-Methylmyristoyl-CoA
show the reaction diagram
-
r
-
-
?
(S)-ibuprofenoyl-CoA
(R)-ibuprofenoyl-CoA
show the reaction diagram
-
-
-
-
?
(S)-Pristanoyl-CoA
(R)-Pristanoyl-CoA
show the reaction diagram
(S)-Trihydroxycoprostanoyl-CoA
(R)-Trihydroxycoprostanoyl-CoA
show the reaction diagram
3alpha,7alpha,12alpha-trihydroxycholestanoyl-CoA
?
show the reaction diagram
-
-
-
-
?
pristanoyl-CoA
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2S)-2-methylacyl-CoA
(2R)-2-methylacyl-CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(11E)-12-iodo-2-methylidenedodec-11-enoyl-CoA
-
-
(24S,25R)-(3R,7R,12R)-trihydroxy-24-fluoro-5beta-cholestan-26-oyl-CoA
-
competitive inhibition
(2R,3S)-3-fluoro-2-methylhexadecanoyl-CoA
-
competitive inhibition
(2S,3R)-3-fluoro-2-methylhexadecanoyl-CoA
-
competitive inhibition
(R)-ibuprofenoyl-CoA
-
competitive inhibition
(S)-ibuprofenoyl-CoA
-
competitive inhibition
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide
-
-
13-iodo-2-methylentridec-12-enoic acid
-
-
14-fluoro-2-methylidenetetradecanoyl-CoA
-
-
2-(4-Isobutylphenyl)propionic acid
2-(trifluoromethyl)tetradecanoyl-CoA
-
-
2-difluoromethylpentadecanoyl-CoA
-
competitive inhibition
2-methylidenetetradecanoyl-CoA
-
-
2-methylmyristoyl CoA
-
competitive inhibition
2-methylmyristoyl-CoA
2-methyloctanoyl CoA
-
competitive inhibition
2-methyloctanoyl-CoA
2-trifluoromethyltetradecanoic acid
-
competitive inhibition
2-trifluoromethyltetradecanoyl-CoA
-
competitive inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
inhibition is reversed by incubation of the inactivated enzyme with 10 mM dithiothreitol
alpha-trifluoromethyltetradecanoic acid
-
inhibits growth of cancer cell lines PC3, CWR22 Rv1, and Du145 in a dose-dependent manner due to AMACR inhibition
beta-fluorinated branched chain alpha-methylacyl coenzyme A esters analogues
-
reversible competitive inhibitors, presence of beta-fluorine on the alpha-methyl group or the acyl chain results in a significant lowering of the Ki value compared with nonfluorinated analogs, and this is attributed to a lowering of the pKa of the alpha-proton, facilitating enolization and binding, competitive
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diethylpyrocarbonate
-
-
diisopropylphosphofluoridate
-
-
dodecylpropanedioyl-CoA
-
-
Fe2+
-
slight inhibition
myristoyl-CoA
-
-
NEM
-
weak
palmitoyl-CoA
thimerosal
-
slight
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
palmitoyl-CoA
-
stimulates at low concentrations, inhibits above 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.076
pristanoyl-CoA
-
-
0.06
trihydroxycoprostanoyl-CoA
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038
(24S,25R)-(3R,7R,12R)-trihydroxy-24-fluoro-5beta-cholestan-26-oyl-CoA
-
pH 7.0, 37°C
0.0013
(2R,3S)-3-fluoro-2-methylhexadecanoyl-CoA
-
pH 7.0, 37°C
0.0023
(2S,3R)-3-fluoro-2-methylhexadecanoyl-CoA
-
pH 7.0, 37°C
0.0054
(R)-ibuprofenoyl-CoA
-
pH 7.0, 37°C
0.0192
(S)-ibuprofenoyl-CoA
-
pH 7.0, 37°C
0.02
2-difluoromethylpentadecanoyl-CoA
-
pH 7.0, 37°C
0.137
2-methylmyristoyl CoA
-
pH 7.0, 37°C
0.045
2-methyloctanoyl CoA
-
pH 7.0, 37°C
0.0009
2-trifluoromethyltetradecanoyl-CoA
-
pH 7.0, 37°C
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
pristanoyl-CoA
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
AMACR is involved in the beta-oxidation of the dietary branched-chain fatty acids and bile acid intermediate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMACR_RAT
382
0
41828
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44700
-
gel filtration
44900
-
1 * 44900, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
-
the enzyme is partially validated as a potential therapeutic target by siRNA knockdown of the AMACR gene, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmitz, W.; Fingerhut, R.; Conzelmann, E.
Purification and properties of an alpha-methylacyl-CoA racemase from rat liver
Eur. J. Biochem.
222
313-323
1994
Rattus norvegicus
Manually annotated by BRENDA team
Schmitz, W.; Albers, C.; Fingerhut, R.; Conzelmann, E.
Purification and characterization of an alpha-methylacyl-CoA racemase from human liver
Eur. J. Biochem.
231
815-822
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Schmitz, W.; Helander, H.M.; Hiltunen, J.K.; Conzelmann, E.
Molecular cloning of cDNA species for rat and mouse liver alpha-methylacyl-CoA racemase
Biochem. J.
326
883-889
1997
Mus musculus (O09174), Mus musculus, Rattus norvegicus (P70473)
Manually annotated by BRENDA team
Van Veldhoven, P.P.; Croes, K.; Casteels, M.; Mannaerts, G.P.
2-Methylacyl racemase: a coupled assay based on the use of pristanoyl-CoA oxidase/peroxidase and reinvestigation of its subcellular distribution in rat and human liver
Biochim. Biophys. Acta
1347
62-68
1997
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Cuebas, D.A.; Phillips, C.; Schmitz, W.; Conzelmann, E.; Novikov, D.K.
The role of alpha-methylacyl-CoA racemase in bile acid synthesis
Biochem. J.
363
801-807
2002
Rattus norvegicus
Manually annotated by BRENDA team
Carnell, A.J.; Hale, I.; Denis, S.; Wanders, R.J.; Isaacs, W.B.; Wilson, B.A.; Ferdinandusse, S.
Design, synthesis, and in vitro testing of alpha-methylacyl-CoA racemase inhibitors
J. Med. Chem.
50
2700-2707
2007
Rattus norvegicus
Manually annotated by BRENDA team
Morgenroth, A.; Urusova, E.A.; Dinger, C.; Al-Momani, E.; Kull, T.; Glatting, G.; Frauendorf, H.; Jahn, O.; Mottaghy, F.M.; Reske, S.N.; Zlatopolskiy, B.D.
New molecular markers for prostate tumor imaging: a study on 2-methylene substituted fatty acids as new AMACR inhibitors
Chemistry
17
10144-10150
2011
Rattus norvegicus, Homo sapiens (Q9UHK6)
Manually annotated by BRENDA team