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Information on EC 2.3.3.10 - hydroxymethylglutaryl-CoA synthase and Organism(s) Gallus gallus and UniProt Accession P23228

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Gallus gallus
UNIPROT: P23228 not found.
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The taxonomic range for the selected organisms is: Gallus gallus
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
3-hydroxy-3-methylglutaryl-coenzyme A synthase
-
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating)
-
-
-
-
3-hydroxy-3-methylglutaryl CoA synthetase
-
-
-
-
3-hydroxy-3-methylglutaryl coenzyme A synthase
-
-
-
-
3-hydroxy-3-methylglutaryl coenzyme A synthetase
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA synthase
-
-
-
-
3-hydroxy-3-methylglutaryl-coenzyme A synthase
-
-
-
-
acetoacetyl coenzyme A transacetase
-
-
-
-
beta-hydroxy-beta-methylglutaryl-CoA synthase
-
-
-
-
HMG-CoA synthase
-
-
-
-
hydroxymethylglutaryl CoA synthetase
-
-
-
-
hydroxymethylglutaryl coenzyme A synthase
-
-
-
-
hydroxymethylglutaryl coenzyme A-condensing enzyme
-
-
-
-
hydroxymethylglutaryl-coenzyme A synthase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
hydrolysis
-
-
-
-
Acyl group transfer
-
-
-
-
transacetylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetoacetyl-CoA C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-44-5
-
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-CoA + H2O + acetoacetyl-CoA
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
-
-
-
?
3-oxobutyryl-CoA + acetoacetyl-CoA + H2O
3-hydroxy-3-methyl-5-oxoheptanedioyl-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
-
-
-
-
?
acetyl-CoA + 3'-dephospho-CoA + H2O
acetyldephospho-CoA + CoA
show the reaction diagram
acetyl-CoA + acetoacetyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
acetyl-CoA + cysteamine + H2O
? + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
acetyl-CoA + N-acetyl-S-acetoacetylcysteamine + H2O
? + CoA
show the reaction diagram
-
-
-
-
?
H2O + acetyl-CoA + S-(3-oxobutyl)-CoA
CoA + S-(4-carboxy-3-hydroxy-isoamyl)-CoA
show the reaction diagram
-
-
-
-
r
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
acetyl-CoA + acetoacetyl-CoA + H2O
(S)-3-hydroxy-3-methylglutaryl-CoA + CoA
show the reaction diagram
acetyl-CoA + H2O + acetoacetyl-CoA
(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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
increases acetoacetate synthesis activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
3-carboxy-2,2,5,5,-tetramethyl-1-pyrrolidinyloxyl-CoA
3-chloropropionyl-CoA
5,5'-dithiobis(2-nitrobenzoate)
-
Ellman's reagent
acetoacetyl-CoA
DL-3-hydroxy-3-methylglutaryl-CoA
Lifibrol
-
-
Mg2+
-
mitochondrial enzyme
MgCl2
-
synthase I
p-chloromercuribenzoate
-
-
palmitoyl-CoA
-
mitochondrial synthase
succinyl-CoA
-
mitochondrial synthase, 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MgCl2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00035 - 0.115
acetoacetyl-CoA
0.0078 - 1.561
acetyl-CoA
0.019 - 0.116
S-(3-oxobutyl)-CoA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0667
acetyl-CoA
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
3-chloropropionyl-CoA
-
-
0.006 - 0.012
acetoacetyl-CoA
0.012
DL-3-hydroxy-3-methylglutaryl-CoA
-
-
0.0005
palmityl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00083
-
mitochondrial pellet
0.00133
-
mitochondrial pellet, 0.25 M sucrose
0.00245
-
disrupted mitochondria, 0.25 M sucrose
0.00288
-
mitochondrial pellet, 0.50 M sucrose
0.00325
-
mitochondrial pellet, 0.88 M sucrose
0.00485
-
homogenate
0.00567
-
disrupted mitochondria, 0.50 M sucrose
0.00792
-
disrupted mitochondria, 0.88 M sucrose
0.00922
-
mitochondrial supernatant
0.00958
-
mitochondrial supernatant, 0.88 M sucrose
0.0101
-
-
0.01053
-
mitochondrial supernatant, 0.50 M sucrose
0.0111
-
mitochondrial supernatant, 0.25 M sucrose
0.5 - 1
-
liver enzyme
0.65
-
cytoplasmic enzyme, isozyme III and IV
0.8 - 1
-
recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.2
-
synthase II
9.3
-
synthase I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.75 - 9.5
-
-
8 - 9.6
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
synthases I, II and III
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HMCS1_CHICK
522
0
57559
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
105000
-
sedimentation equlibrium
116000
gel filtration
52000
-
2 * 52000, mitochondrial synthase, synthase I, SDS-PAGE
53000
55000
-
2 * 55000, synthase II, SDS-PAGE
57000
-
2 * 57000, gel filtration
57490
-
deduced amino acid sequence
57600
58000
-
2 * 58000, synthases III and IV, SDS-PAGE
88000
-
gel filtration
90000
-
gel filtration, synthase I
94000 - 100000
-
gel filtration, synthase II
96000
-
gel filtration
96000 - 105000
-
gel filtration, mitochondrial synthase
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is vulnerable to proteolysis, expression in Escherichia coli leads to an quite stable enzyme
-
relatively stable dialyzed against 10 mM potassium phosphate in 0.1 mM dithiothreitol and EDTA for 4-10 days
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, may be stored in 30% glycerin solution for 2-3 months with no loss of activity
-
-20°C, purified synthase may be stored for 2-3 months with little loss of activity by adding 30% glyerol
-
-80°C, recombinant enzyme, negligible loss of activity after 1 year
-
-85°C, in presence of 30% glycerol stable for over 1 year
-
-90°C, purified synthases II-IV in 20 mM potassium phosphate, pH 7.0, 5 mM dithiothreitol, can be stored as pellets following precipitation by 60% saturated ammonium sulfate up to 3 months without loss of activity
-
0°C, purified synthase I stored frozen in 40% glycerol containing 20 mM potassium phosphate, pH 7.0, 5 mM dithiothreitol, stable for 3-4 months
-
4°C, in presence of 30% glycerol stable for several days
-
4°C, purified synthase I stored in 40% glycerol containing 20 mM potassium phosphate, pH 7.0, 5 mM dithiothreitol is unstable
-
4°C, purified synthases II-IV in 20 mM potassium phosphate, pH 7.0, 5 mM dithiothreitol, stable for several weeks
-
4°C, recombinant enzyme, loses 50% activity after 1 year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic synthase
-
mitochondrial form
-
partially
-
recombinant enzyme, expressed in Escherichia coli
-
several mutants partially purified
synthase species I-IV
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned and sequenced
-
expression vector pET-3d, cloned and expressed in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allred, J.B.
Properties and subcellular distribution of enzymes required for acetoacetate biosynthesis in chicken liver
Biochim. Biophys. Acta
297
22-30
1973
Cavia porcellus, Gallus gallus, 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
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
Reed, W.D.; Clinkenbeard, K.D.; Lane, M.D.
Molecular and catalytic properties of mitochondrial (ketogenic) 3-hydroxy-3-methylglutaryl coenzyme A synthase of liver
J. Biol. Chem.
250
3117-3123
1975
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Reed, W.D.; Lane, M.D.
Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase from chicken liver
Methods Enzymol.
35 B
155-160
1975
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
Menahan, L.A.; Hron, W.T.; Hinkelman, D.G.; Miziorko, H.M.
Interrelationships between 3-hydroxy-3-methylglutaryl-CoA synthase, aetoacetyl-CoA and ketogenesis
Eur. J. Biochem.
119
287-296
1981
Gallus gallus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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
Miziorko, H.M.; Behnke, C.E.
Active-site directed inhibition of 3-hydroxy-3-methylglutaryl coenzyme A synthase by 3-chloropropionyl coenzyme A
Biochemistry
34
3174-3179
1985
Gallus gallus
-
Manually annotated by BRENDA team
Greenspan, M.D.; Yudkovitz, J.B.; Lo, C.Y.L.; Chen, J.S.; Alberts, A.W.; Hunt, V.M.; Chang, M.N.; Yang, S.S.; Thompson, K.L.; Chiang, Y.C.P.; Chabala, J.C.; Monaghan, R.L.; Schwartz, R.L.
Inhibition of hydroxymethylglutaryl-coenzyme A synthase by L659,699
Proc. Natl. Acad. Sci. USA
84
7488-7492
1987
Gallus gallus, Cricetulus griseus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Miziorko, H.M.
3-Hydroxy-3-methylglutaryl-CoA synthase from chicken liver
Methods Enzymol.
110
19-26
1988
Gallus gallus
Manually annotated by BRENDA team
Misra, I.; Narasimhan, C.; Miziorko, H.M.
Avian 3-hydroxy-3-methylglutaryl-CoA synthase
J. Biol. Chem.
268
12129-12135
1993
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Rokosz, L.L.; Boulton, D.A.; Butkiewicz, E.A.; Sanyal, G.; Cueto, M.A.; Lachance, P.A.; Hermes, J.D.
Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, andcharacterization of recombinant wild-type and cys-129 mutant enzymes
Arch. Biochem. Biophys.
312
1-13
1994
Gallus gallus, Cricetulus griseus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Misra, I.; Charlier, H.A.; Miziorko, H.M.
Avian cytosolic 3-hydroxy-3-methylglutaryl-CoA synthase. Evaluation of the role of cysteines in reaction chemistry
Biochim. Biophys. Acta
1247
253-259
1995
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Cricetulus griseus (P13704), Blattella germanica (P54870), Blattella germanica (P54961)
Manually annotated by BRENDA team
Montamat, F.; Guilloton, M.; Karst, F.; Delrot, S.
Isolation and characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl-coenzyme A synthase
Gene
167
197-201
1995
Arabidopsis thaliana, Catharanthus roseus, Gallus gallus, Cricetulus griseus, Homo sapiens, Raphanus sativus, Rattus norvegicus
Manually annotated by BRENDA team
Scharnagl, H.; Mrz, W.; Schliack, M.; Lser, R.; Gross, W.
A novel assay of cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase activity using reversed-phase ion-pair chromatography: demonstration that Lifibrol (K12.148) modulates the enzyme activity
J. Lipid Res.
36
622-627
1995
Bos taurus, Gallus gallus, Cricetulus griseus, Homo sapiens, Mesocricetus auratus, Rattus norvegicus
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
Chun, K.Y.; Vinarov, D.A.; Zajicek, J.; Miziorko, H.M.
3-hydroxy-3-methylglutaryl-CoA synthase. A role for glutamate 95 in general acid/base catalysis of C-C bond formation
J. Biol. Chem.
275
17946-17953
2000
Gallus gallus, Gallus gallus (P23228), Homo sapiens, Homo sapiens (P54868), Methanothermobacter thermautotrophicus, Sus scrofa (O02734), Borreliella burgdorferi (O51626), Rattus norvegicus (P22791), Mus musculus (P54869), Blattella germanica (P54870), Blattella germanica (P54961), Arabidopsis thaliana (P54873), Schizosaccharomyces pombe (P54874), Pinus sylvestris (P93773)
Manually annotated by BRENDA team
Vinarov, D.A.; Miziorko, H.M.
3-Hydroxy-3-methylglutaryl-coenzyme A synthase reaction intermediates: Detection of a covalent tetrahedral adduct by differential isotope shift 13C nuclear magnetic resonance spectroscopy
Biochemistry
39
3360-3368
2000
Gallus gallus
Manually annotated by BRENDA team
Sutherlin, A.; Hedl, M.; Sanchez-Neri, B.; Burgner, J.W.; Stauffacher, C.V.; Rodwell, V.W.
Enterococcus faecalis 3-hydroxy-3-methylglutaryl coenzyme A synthase, an enzyme of isopentenyl diphosphate biosynthesis
J. Bacteriol.
184
4065-4070
2002
Blattella germanica, Borreliella burgdorferi, Bos taurus, Streptomyces sp., Gallus gallus, Streptococcus pneumoniae, Enterococcus faecalis, Homo sapiens, Mesocricetus auratus, Staphylococcus aureus, Mus musculus, Rattus norvegicus, Staphylococcus epidermidis, Staphylococcus haemolyticus, Streptococcus pyogenes, Sus scrofa
Manually annotated by BRENDA team
Misra, I.; Wang, C.Z.; Miziorko, H.M.
The influence of conserved aromatic residues in 3-hydroxy-3-methylglutaryl-CoA synthase
J. Biol. Chem.
12
12
2003
Gallus gallus
-
Manually annotated by BRENDA team
Liao, P.; Wang, H.; Hemmerlin, A.; Nagegowda, D.A.; Bach, T.J.; Wang, M.; Chye, M.L.
Past achievements, current status and future perspectives of studies on 3-hydroxy-3-methylglutaryl-CoA synthase (HMGS) in the mevalonate (MVA) pathway
Plant Cell Rep.
33
1005-1022
2014
Arabidopsis thaliana (P54873), Brassica juncea (Q9M6U3), Camptotheca acuminata (B3GDB1), Catharanthus roseus, Gallus gallus (P23228), Hevea brasiliensis (Q94ET0), Hevea brasiliensis, Homo sapiens (A0A024R059), Melampsora larici-populina, Mesocricetus auratus, Pinus sylvestris (P93773), Populus trichocarpa x Populus deltoides, Rattus norvegicus (P17425), Salvia miltiorrhiza (D2DS62), Solanum lycopersicum (A9LRT6), Sus scrofa (O02734), Taxus x media (Q693N8)
Manually annotated by BRENDA team