Information on EC 5.1.99.4 - alpha-Methylacyl-CoA racemase

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

EC NUMBER
COMMENTARY hide
5.1.99.4
-
RECOMMENDED NAME
GeneOntology No.
alpha-Methylacyl-CoA racemase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bile acid biosynthesis, neutral pathway
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
-
Metabolic pathways
-
-
Primary bile acid biosynthesis
-
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
strain P101
-
-
Manually annotated by BRENDA team
strain P101
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(25R)-trihydroxycoprostanoyl-CoA
(25S)-trihydroxycoprostanoyl-CoA
show the reaction diagram
-
-
-
-
?
(25S)-3,7,12-trihydroxycoprostanoic acid
(25R)-3,7,12-trihydroxycoprostanoic acid
show the reaction diagram
-
-
-
r
(25S)-trihydroxycoprostanoyl-CoA
(25R)-trihydroxycoprostanoyl-CoA
show the reaction diagram
-
-
-
-
?
(2R)-ibuprofenoyl-CoA
(2S)-ibuprofenoyl-CoA
show the reaction diagram
-
-
-
-
r
(2R)-pristanoyl-CoA
(2S)-pristanoyl-CoA
show the reaction diagram
-
-
-
-
r
(2S)-2-methylacyl-CoA
(2R)-2-methylacyl-CoA
show the reaction diagram
(2S)-pristanoyl-CoA
(2R)-pristanoyl-CoA
show the reaction diagram
(R)-2-methyldecanoyl-CoA
(S)-2-methyldecanoyl-CoA
show the reaction diagram
-
-
-
-
r
(R)-2-methylpentadecanoyl-CoA
(S)-2-methylpentadecanoyl-CoA
show the reaction diagram
(R)-2-methyltetradecanoyl-CoA
(S)-2-methyltetradecanoyl-CoA
show the reaction diagram
-
-
-
-
r
(R)-fenoprofenoyl-CoA
(S)-fenoprofenoyl-CoA
show the reaction diagram
-
best substrate
-
-
?
(R)-ibuprofenoyl-CoA
(S)-ibuprofenoyl-CoA
show the reaction diagram
(R)-pristanoyl-CoA
(S)-pristanoyl-CoA
show the reaction diagram
(S)-2-methyldecanoyl-CoA
(R)-2-methyldecanoyl-CoA
show the reaction diagram
(S)-2-Methylmyristoyl-CoA
(R)-2-Methylmyristoyl-CoA
show the reaction diagram
(S)-2-Methyltetradecanoyl-CoA
(R)-2-Methyltetradecanoyl-CoA
show the reaction diagram
-
r
-
-
-
(S)-ibuprofenoyl-CoA
(R)-ibuprofenoyl-CoA
show the reaction diagram
(S)-ketoprofenoyl-CoA
(R)-ketoprofenoyl-CoA
show the reaction diagram
-
-
-
-
?
(S)-naproxenoyl-CoA
(R)-naproxenoyl-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-trihydroxy-5beta-cholestanoyl-CoA
?
show the reaction diagram
-
-
-
-
?
3alpha,7alpha,12alpha-trihydroxycholestanoyl-CoA
?
show the reaction diagram
flurbiprofenoyl-CoA
?
show the reaction diagram
-
-
-
-
?
S-[(2R)-2-methyl-6-[(3alpha,5beta,7alpha)-3,7,12-trihydroxy-10-methylgonan-17-yl]heptanoyl]-CoA
S-[(2S)-2-methyl-6-[(3alpha,5beta,7alpha)-3,7,12-trihydroxy-10-methylgonan-17-yl]heptanoyl]-CoA
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
INHIBITORS
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
(25-R,S)-3,7,12-trihydroxycoprostanoic acid
competitive inhibition
(2R)-ibuprofenoyl-CoA
-
competitive inhibitor
(2R,3S)-3-fluoro-2-methylhexadecanoyl-CoA
-
competitive inhibition
(2S)-ibuprofenoyl-CoA
-
competitive inhibitor
(2S,3R)-3-fluoro-2-methylhexadecanoyl-CoA
-
competitive inhibition
(4-tert-butylphenyl)(chloro)acetyl-CoA
-
-
(R)-2-methylmyristoyl CoA
binding mode
(R)-ibuprofenoyl-CoA
-
competitive inhibition
(R,S)-ibuprofenoyl-CoA
competitive inhibition
(S)-2-methylmyristoyl CoA
binding mode
(S)-ibuprofenoyl-CoA
1-(4-methylphenyl)ethanone
-
-
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide
-
-
13-iodo-2-methylentridec-12-enoic acid
14-fluoro-2-methylidenetetradecanoyl-CoA
2-(4-Isobutylphenyl)propionic acid
2-(4-tert-butylphenyl)-2-fluoropropanoyl-CoA
-
-
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
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
amidocarboxymethyl-dethia-CoA
-
-
-
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
-
carboxymethyl-dethia-CoA
-
-
-
decanoyl-CoA
-
non-competitive substrate inhibition at higher substrate concentrations
Diethylpyrocarbonate
-
-
diisopropylphosphofluoridate
-
-
dodecyl(methyl)carbamoyl-CoA
-
-
dodecylcarbamoyl-CoA
-
-
dodecylpropanedioyl-CoA
Fe2+
-
slight inhibition
Ibuprofen
-
chemopreventive effects of ibuprofen on prostate cancer risk, which may be enhanced by AMACR genetic variants
ibuprofenoyl-CoA
-
competitive versus substrate trihydroxycoprostanoyl-CoA
-
myristoyl-CoA
N-acetylamino-4-methylacetophenone
-
-
N-dodecanoyl-D-alanyl-CoA
-
-
N-methylthiocarbamate
-
-
-
NEM
-
weak
octyl-beta-D-glucopyranoside
-
concentrations greater than 0.6% octyl-beta-D-glucopyranoside cause a reduction in enzyme activity
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
0.048 - 0.071
(2R)-ibuprofenoyl-CoA
0.277
(2S)-2-methyldecanoyl-CoA
-
pH and temperature not specified in the publication
0.086 - 0.087
(2S)-ibuprofenoyl-CoA
1.2
(R)-2-methyldecanoyl-CoA
-
recombinant enzyme, 50 mM NaH2PO4-NaOH, pH 7.2
0.041
(R)-Pristanoyl-CoA
-
wild type
0.614 - 1.2
(S)-2-methyldecanoyl-CoA
0.052
(S)-ketoprofenoyl-CoA
-
pH and temperature not specified in the publication
0.068
(S)-naproxenoyl-CoA
-
pH and temperature not specified in the publication
0.076 - 0.172
pristanoyl-CoA
0.0316 - 0.06
trihydroxycoprostanoyl-CoA
additional information
additional information
-
similar Km values for mutants H126A, D156A and E241A as for the wild-type
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
228 - 291
(2R)-ibuprofenoyl-CoA
0.031
(2S)-2-methyldecanoyl-CoA
Homo sapiens
-
pH and temperature not specified in the publication
358 - 450
(2S)-ibuprofenoyl-CoA
53.8
(R)-2-methyldecanoyl-CoA
Homo sapiens
-
recombinant enzyme, 50 mM NaH2PO4-NaOH, pH 7.2
0.07 - 60.9
(S)-2-methyldecanoyl-CoA
0.015
(S)-ketoprofenoyl-CoA
Homo sapiens
-
pH and temperature not specified in the publication
0.0095
(S)-naproxenoyl-CoA
Homo sapiens
-
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032 - 0.0061
(2R)-ibuprofenoyl-CoA
0.112
(2S)-2-methyldecanoyl-CoA
Homo sapiens
-
pH and temperature not specified in the publication
41729
0.0041 - 0.0052
(2S)-ibuprofenoyl-CoA
44.8
(R)-2-methyldecanoyl-CoA
Homo sapiens
-
recombinant enzyme, 50 mM NaH2PO4-NaOH, pH 7.2
27241
0.114 - 50.75
(S)-2-methyldecanoyl-CoA
0.29
(S)-ketoprofenoyl-CoA
Homo sapiens
-
pH and temperature not specified in the publication
41727
0.14
(S)-naproxenoyl-CoA
Homo sapiens
-
pH and temperature not specified in the publication
41728
additional information
additional information
Mycobacterium tuberculosis
-
Mycobacterium tuberculosis enzyme expressed as a fusion protein bearing an N-terminal six-His tag has a catalytic efficiency that is reduced 22% and 47% in the 2S-2R and 2R-2S directions, respectively, relative to untagged enzyme
2
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, 37C
0.0013
(2R,3S)-3-fluoro-2-methylhexadecanoyl-CoA
-
pH 7.0, 37C
0.0023
(2S,3R)-3-fluoro-2-methylhexadecanoyl-CoA
-
pH 7.0, 37C
0.000575
(4-tert-butylphenyl)(chloro)acetyl-CoA
-
pH not specified in the publication, 37C
0.0054
(R)-ibuprofenoyl-CoA
-
pH 7.0, 37C
0.0192
(S)-ibuprofenoyl-CoA
-
pH 7.0, 37C
0.000254
2-(4-tert-butylphenyl)-2-fluoropropanoyl-CoA
-
pH not specified in the publication, 37C
0.02
2-difluoromethylpentadecanoyl-CoA
-
pH 7.0, 37C
0.137
2-methylmyristoyl CoA
-
pH 7.0, 37C
0.045
2-methyloctanoyl CoA
-
pH 7.0, 37C
0.000156 - 0.0009
2-trifluoromethyltetradecanoyl-CoA
0.000028
amidocarboxymethyl-dethia-CoA
-
pH not specified in the publication, 37C
-
0.0000016
carboxymethyl-dethia-CoA
-
pH not specified in the publication, 37C
-
0.000098
dodecyl(methyl)carbamoyl-CoA
-
pH not specified in the publication, 37C
0.000001
dodecylcarbamoyl-CoA
-
pH not specified in the publication, 37C
0.0000023
N-dodecanoyl-D-alanyl-CoA
-
pH not specified in the publication, 37C
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.21
-
mutant P1
68.4
-
substrate is (R)-2-methyldecanoyl-CoA, recombinant enzyme, 50 mM NaH2PO4-NaOH, pH 7.2
77.5
-
substrate is (S)-2-methyldecanoyl-CoA, recombinant enzyme, 50 mM NaH2PO4-NaOH, pH 7.2
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
pristanoyl-CoA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
more than 80% of maximal activity between pH 6.5 and pH 9.0, inactive below pH 5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.07
isoenzyme IA, calculated
7.01
-
calculated
9.44
isoenzyme IIB, calculated
9.62
isoenzyme IIA, calculated
9.65
isoenzyme IIAs, calculated
10.31
isoenzyme IB, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
epithelium that is negative for dysplasia and columnar epithelial cell changes indefinite for dysplasia does not demonstrate immunoreactivity for alpha-methylacyl-Coa racemase. Barrett's epithelium with columnar epithelial cell changes indefinite for dysplasia demonstrates alpha-methylacyl-Coa racemase immunoreactivity in 30% of cases
Manually annotated by BRENDA team
-
dysplastic Barretts epithelium, immunohistochemic detection
Manually annotated by BRENDA team
-
upper urinary tract urothelial carcinomas
Manually annotated by BRENDA team
-
weak
Manually annotated by BRENDA team
-
immunohistochemic detection
Manually annotated by BRENDA team
-
patients with chronic inflammatory disease prostate carcinoma
Manually annotated by BRENDA team
-
staining for alpha-methylacyl-CoA racemase is uniformly negative in samples negative for dysplasia and indefinite for dysplasia. In the groups of high-grade dysplasia and invasive intestinal-type adenocarcinoma, 76% and 34% of samples are positive for alpha-methylacyl-CoA racemase, respectively. Expression of alpha-methylacyl-CoA racemase is not correlated with location, Helicobacter pylori infection, or intestinal metaplasia
Manually annotated by BRENDA team
-
weak
Manually annotated by BRENDA team
-
immunohistochemic detection and expression analysis, pattern and distribution, overview
Manually annotated by BRENDA team
-
from a renal neoplasm
Manually annotated by BRENDA team
-
weak
Manually annotated by BRENDA team
-
type 1 and type 2 papillary, conventional, and chromophobe renal cell carcinoma, oncocytomas, mucinous tubular and spindle tumors, urothelial carcinomas, angiomyolipomas, and Bellini carcinomas, immunohistochemical analysis of enzyme expression, overview
Manually annotated by BRENDA team
-
samples of normal adult glands as well as cases of sebaceous hyperplasia, sebaceous adenoma, and basal cell carcinoma with sebaceous differentiation and extraocular sebaceous carcinoma
Manually annotated by BRENDA team
-
patients with AMACR-positive SCLC show a better survival rate
Manually annotated by BRENDA team
-
weak
Manually annotated by BRENDA team
-
weak
Manually annotated by BRENDA team
-
weak
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22200
isoenzyme IB, calculated
28470
isoenzyme IIAs, calculated
30790
isoenzyme IIB, calculated
31650
isoenzyme IIA, calculated
38970
-
calculated for recombinant enzyme without six-His tag
39000
-
SDS-PAGE
40850
-
calculated for recombinant enzyme with six-His tag
42390
isoenzyme IA, calculated
43830
-
calculated from amino acid sequence
44700
-
gel filtration
45000
-
determined by SDS-PAGE
47150
-
calculated fpor His-tagged protein
47700
-
gel filtration
75000
-
dynamic light-scattering measurement
89000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 39000, SDS-PAGE
monomer
additional information
structure of the enzyme in complex with acetyl-CoA, acetoacetyl-CoA, (R,S)-ibuprofenoyl-CoA, (2S)-methylmyristoyl-CoA, or (2R)-methylmyristoyl-CoA, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.8 A resolution
-
hanging-drop vapour-diffusion method, the best crystals grow in 1.26 M ammonium phosphate, pH 7.0 using a protein concentration of 24 mg/ml
-
purified recombinant wild-type enzyme in complex with acetyl-CoA, acetoacetyl-CoA, (R,S)-ibuprofenoyl-CoA, (2S)-methylmyristoyl-CoA, or (2R)-methylmyristoyl-CoA, 22C, hanging-drop vapor-diffusion method, with reservoir solution containing 1.52 M ammonium phosphate, 10 mM BaCl2 at pH 7.0 in 0.0066 ml drops containing a 1:1 v/v mixture of reservoir and protein solution, the latter containing 6 mg/ml in 10 mM potassium phosphate buffer, pH 8.8, X-ray diffraction structure determination and analysis at 1.6-2.3 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 40
-
slow loss of activity
50
-
half-life: 15 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by using metal ion affinity chromatography
-
purification by affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AMACR 1A, the major splice variant, is expressed as a His-tag protein in Escherichia coli cells
-
expression in COS-7 cells
-
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
genotyping, determination of five non-synonymous and two intronic AMACR polymorphisms, no associations between the genetic variants and prostate cancer, overview
-
genotyping, determination of five single nucleotide polymorphisms tagging common haplotype variation within the coding and regulatory regions of AMACR, the risk of familial, but not sporadic, prostate cancer may be associated with germline variation in the AMACR gene, overview
-
overexpression in Escherichia coli
the open reading frame encoding alpha-methylacyl-coenzyme A racemase from Mycobacterium tuberculosis is subcloned into a pET15b vector, and the enzyme is overexpressed in Escherichia coli cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AMACR is negative in postatrophic hyperplasia, mucinous metaplasia, and urothelial metaplasia
-
AMACR is overexpressed in prostate cancer
-
coexpression of alpha-methylacyl coenzyme A racemase and nuclear p53 in neoplastic lesions
-
decreasing alpha-methylacyl-CoA racemase expression in tumors with less sebaceous differentiation, these findings provide insight into the potential pathogenesis of sebaceous neoplasms while assisting in the microscopic distinction of sebaceous adenoma from sebaceous carcinoma
-
enzyme is over-expressed in prostate and other cancers
-
enzyme is strongly expressed in prostate cancer cell lines and tissues as compared with benign or normal prostate tissues, furthermore, enzyme is expressed abundantly in colorectal cancer, lung cancer tissues, renal and hepatic cancer, whereas it is barely detected in benign tissues and normal prostate epithelial cells
-
in addition to the over-expression in prostate carcinoma, enzyme is also over-expressed in a number of adenocarcinomas, notably colorectal carcinoma as well as in hepatocellular and renal cell carcinoma
-
partial atrophy shows negative and weak expression of alpha-methylacyl coenzyme A racemase in 75.3% and 24.7% acini, the secretory compartment in all variants of complete atrophy shows alpha-methylacyl coenzyme A racemase negative expression
-
patients with benign prostate hyperplasia have negative expression of AMACR
-
positive AMACR immunehistochemistry staining is strongly associated with neoplastic transformation of the colon epithelium, AMACR positively is observed in the majority of invasive cancers and histologically recognized dysplasias
-
the expression of alpha-methylacyl-CoA racemase is increased in benign sebaceous glands and sebaceous hyperplasia
-
transcript levels of most AMACR splice variants are significantly upregulated in prostate cancer compared with its adjacent normal counterparts (in the order: IA>> IAd = IIA>> IIAs> IAs), while splice variant IB is the most abundant form of B variant and expression of splice variant IIB is negligible
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C297A
-
mutant with 6.2% relative enzyme activity
D127A
-
mutant with 21.6% relative enzyme activity
D156A
-
mutant with 17.6% relative enzyme activity
D185A
-
mutant with 68.5% relative enzyme activity
D190A
-
mutant with 3.3% relative enzyme activity
D231A
-
mutant with 25.0% relative enzyme activity
D28A
-
mutant with 24.2% relative enzyme activity
D60A
-
mutant with 22.7% relative enzyme activity
D78A
-
mutant with 44.0% relative enzyme activity
E241A
-
mutant with 2.1% relative enzyme activity
E306A
-
mutant with 23.1% relative enzyme activity
E82A
-
mutant with 12.5% relative enzyme activity
E90A
-
mutant with 67.0% relative enzyme activity
E97A
-
mutant with 95.4% relative enzyme activity
H126A
-
mutant with 4.5% relative enzyme activity
H312A
-
mutant with 10.1% relative enzyme activity
I56P
-
mutant with 28.8% relative enzyme activity
K62A
-
mutant with 117.6% relative enzyme activity
M111P
-
mutant with 5.2% relative enzyme activity
R175A
-
mutant with 63.6% relative enzyme activity
R38A
-
mutant with 20.9% relative enzyme activity
R52A
-
mutant with 15.7% relative enzyme activity
R54A
-
mutant with 37.4% relative enzyme activity
R85A
-
mutant with 20.3% relative enzyme activity
R91A
-
mutant with 19.9% relative enzyme activity, 9fold increase of Km compared with the wild type
Y130A
-
mutant with 24.7% relative enzyme activity
Y224A
-
mutant with 22.6% relative enzyme activity
Y227A
-
mutant with 20.1% relative enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
drug development
-
AMACR can be an attractive target for cytotoxic T-lymphocyte-based immunotherapy for cancer
medicine
pharmacology
-
the enzyme is partially validated as a potential therapeutic target by siRNA knockdown of the AMACR gene, overview
Show AA Sequence (402 entries)
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