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Information on EC 2.3.3.10 - hydroxymethylglutaryl-CoA synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P54839

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Saccharomyces cerevisiae
UNIPROT: P54839 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hmg-coa, hmg-coa synthase, hmgcs2, hmgs, hmgcs1, 3-hydroxy-3-methylglutaryl-coa synthase, hydroxymethylglutaryl-coa synthase, 3-hydroxy-3-methylglutaryl-coenzyme a synthase, 3-hydroxy-3-methylglutaryl coenzyme a synthase, hmgcs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating)
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3-hydroxy-3-methylglutaryl CoA synthetase
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3-hydroxy-3-methylglutaryl coenzyme A synthase
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3-hydroxy-3-methylglutaryl coenzyme A synthetase
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3-hydroxy-3-methylglutaryl-CoA synthase
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3-hydroxy-3-methylglutaryl-coenzyme A synthase
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acetoacetyl coenzyme A transacetase
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beta-hydroxy-beta-methylglutaryl-CoA synthase
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HMG-CoA synthase
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hydroxymethylglutaryl CoA synthetase
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hydroxymethylglutaryl coenzyme A synthase
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hydroxymethylglutaryl coenzyme A-condensing enzyme
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hydroxymethylglutaryl-coenzyme A synthase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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hydrolysis
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Acyl group transfer
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transacetylation
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetoacetyl-CoA C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-44-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + acetoacetyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
-
-
-
?
acetyl-3'-dephospho-CoA + acetoacetyl-CoA + H2O
3-hydroxy-3-methylglutaryl-CoA + 3'-dephospho-CoA
show the reaction diagram
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-
-
-
?
acetyl-CoA + acetoacetyl-ACP + H2O
3-hydroxy-3-methylglutaryl-ACP
show the reaction diagram
-
-
-
-
?
acetyl-CoA + acetoacetyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
acetylglutathione + acetoacetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
?
acetylpantetheine + acetoacetyl-CoA + H2O
3-hydroxy-3-methylglutaryl-CoA + pantetheine
show the reaction diagram
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-
-
-
?
additional information
?
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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
acetyl-CoA + acetoacetyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + acetoacetyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
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3,3-dimethylglutaryl-CoA
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3-oxohexanoyl-CoA
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5,5'-dithiobis(2-nitrobenzoate)
acetoacetyl-CoA
arsenite
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in presence of CoA, residual activity 25%
bromoacetyl-CoA
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CdSO4
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residual activity 9%
decanoyl-CoA
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DL-3-hydroxy-3-methylglutaryl-CoA
DL-3-methylglutaryl-CoA
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glutaryl-CoA
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heptanoyl-CoA
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hexanoyl-CoA
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iodoacetamide
N-ethylmaleimide
NaAsO2
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residual activity 90%
nonanoyl-CoA
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octanoyl-CoA
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p-chloromercuribenzoate
phenyl arsenious oxide
propionyl-CoA
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-
additional information
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desulfo-CoA protects against bromoacetyl-CoA inhibition, but not against p-chloromercuribenzoate and N-ethylmaleimide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
potassium phosphate
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Sodium phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001 - 0.0032
acetoacetyl-CoA
0.014 - 0.018
acetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
3,3-dimethylglutaryl-CoA
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pH 8.0
0.0071 - 0.014
3-oxohexanoyl-CoA
0.008 - 0.02
acetoacetyl-CoA
0.033
butyryl-CoA
-
pH 8.0
0.038 - 0.06
CoA
0.0027
decanoyl-CoA
-
pH 8.0
0.03 - 0.07
desulfo-CoA
0.013
DL-3-hydroxy-3-methylglutaryl-CoA
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pH 8.0, competitive inhibition, substrate acetyl-CoA
0.1
DL-3-methylglutaryl-CoA
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pH 8.0
0.11
glutaryl-CoA
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pH 8.0
0.0123
heptanoyl-CoA
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pH 8.0
0.022
hexanoyl-CoA
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pH 8.0
0.004
nonanoyl-CoA
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pH 8.0
0.0081
octanoyl-CoA
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pH 8.0
0.005
propionyl-CoA
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pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
baker's yeast
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
cholesterogenic isoform
Manually annotated by BRENDA team
cholesterogenic isoform
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is labile to freezing and thawing, stabilized by glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°, stored in presence of dithiothreitol and 30-50% glycerol purified enzyme retains complete activity for up to 3 months
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4°C, enzyme loses activity in absence of glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Middleton, B.
The kinetic mechanism of 3-hydroxy-3-methylglutaryl-coenzyme a synthase from baker's yeast
Biochem. J.
126
35-47
1972
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Middleton, B.; Tubbs, P.K.
The purification and some properties of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from baker's yeast
Biochem. J.
126
27-34
1972
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Cornforth, J.W.; Phillips, G.T.
Substrate stereochemistry of 3-hydroxy-3-methylglutaryl-coenzyme A synthase
Eur. J. Biochem.
42
591-604
1974
Saccharomyces cerevisiae, Rattus norvegicus
Manually annotated by BRENDA team
Clinkenbeard, K.D.; Sugiyama, T.; Lane, M.D.
Cytosolic 3-hydroxy-3-methylglutaryl-CoA synthase from chicken liver
Methods Enzymol.
35 B
160-167
1975
Saccharomyces cerevisiae, Gallus gallus
-
Manually annotated by BRENDA team
Clinkenbeard, K.D.; Sugiyama, T.; Reed, W.D.; Lane, M.D.
Cyoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase from liver
J. Biol. Chem.
250
3124-3135
1975
Saccharomyces cerevisiae, Gallus gallus, Columba livia, Meleagris gallopavo, Rattus norvegicus
-
Manually annotated by BRENDA team
Middleton, B.; Tubbs, P.K.
3-Hydroxy-3-methylglutaryl-CoA synthase from baker's yeast
Methods Enzymol.
35 B
173-177
1975
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Miziorko, H.M.; Clinkenbeard, K.D.; Reed, W.D.; Lane, M.D.
3-Hydroxy-3-methylglutaryl coenzyme A synthase
J. Biol. Chem.
250
5768-5773
1975
Saccharomyces cerevisiae, Gallus gallus
Manually annotated by BRENDA team
Page, M.A.; Tubbs, P.K.
Some properties of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver
Biochem. J.
173
925-928
1978
Bos taurus, Saccharomyces cerevisiae, Gallus gallus
Manually annotated by BRENDA team
Lowe, D.M.; Tubbs, P.K.
3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver
Biochem. J.
227
591-599
1985
Bos taurus, Saccharomyces cerevisiae, Gallus gallus
Manually annotated by BRENDA team
Misra, I.; Miziorko, H.M.
Evidence for the interaction of avian 3-hydroxy-3-methylglutaryl-CoA synthase H264 with acetoacetyl-CoA
Biochemistry
35
9610-9616
1996
Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Blattella germanica (P54870), Blattella germanica (P54961)
Manually annotated by BRENDA team
Cabano, J.; Buesa, C.; Hegardt, F.G.; Marrero, P.F.
Catalytic properties of recombinant 3-hydroxy-3-methylglutaryl coenzyme A synthase-1 from Blattella germanica
Insect Biochem. Mol. Biol.
27
499-505
1997
Blattella germanica, Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Diploptera punctata, Locusta migratoria
Manually annotated by BRENDA team
Chun, K.Y.; Vinarov, D.A.; Miziorko, H.M.
3-Hydroxy-3-methylglutaryl-CoA synthase: Participation of invariant acidic residues in formation of the acetyl-S-enzyme reaction intermediate
Biochemistry
39
14670-14681
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P54839), Gallus gallus, Gallus gallus (P23228), Homo sapiens, Homo sapiens (P54868), Homo sapiens (Q01581), Mesocricetus auratus, Methanothermobacter thermautotrophicus, Sus scrofa (O02734), Borreliella burgdorferi (O51626), Cricetulus griseus (P13704), Rattus norvegicus (P17425), Rattus norvegicus (P22791), Mus musculus (P54869), Blattella germanica (P54870), Blattella germanica (P54961), Caenorhabditis elegans (P54871), Arabidopsis thaliana (P54873), Schizosaccharomyces pombe (P54874), Pinus sylvestris (P93773)
Manually annotated by BRENDA team