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Literature summary for 2.3.3.10 extracted from

  • VanNice, J.C.; Skaff, D.A.; Wyckoff, G.J.; Miziorko, H.M.
    Expression in Haloferax volcanii of 3-hydroxy-3-methylglutaryl coenzyme A synthase facilitates isolation and characterization of the active form of a key enzyme required for polyisoprenoid cell membrane biosynthesis in halophilic archaea (2013), J. Bacteriol., 195, 3854-3862.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Haloferax volcanii Haloferax volcanii

Inhibitors

Inhibitors Comment Organism Structure
hymeglusin
-
 Haloferax volcanii
methanol
-
 Haloferax volcanii
additional information insensitive to feedback substrate inhibition by acetoacetyl-CoA Haloferax volcanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0014
-
 acetoacetyl-CoA pH 8.0, 30°C Haloferax volcanii
0.05
-
 acetyl-CoA pH 8.0, 30°C Haloferax volcanii

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
KCl optimal concentration Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51975
-
 x * 51975, matrix-assisted laser desorption ionization-time of flight mass spectrometry Haloferax volcanii
65000
-
 x * 65000, SDS-PAGE Haloferax volcanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + H2O + acetoacetyl-CoA Haloferax volcanii the enzyme is involved in the mevalonate pathway. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?
acetyl-CoA + H2O + acetoacetyl-CoA Haloferax volcanii DSM 3757 the enzyme is involved in the mevalonate pathway. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GWR6
-
-
Haloferax volcanii DSM 3757 D4GWR6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + H2O + acetoacetyl-CoA
-
 Haloferax volcanii (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?
acetyl-CoA + H2O + acetoacetyl-CoA the enzyme is involved in the mevalonate pathway. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway Haloferax volcanii (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?
acetyl-CoA + H2O + acetoacetyl-CoA
-
 Haloferax volcanii DSM 3757 (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?
acetyl-CoA + H2O + acetoacetyl-CoA the enzyme is involved in the mevalonate pathway. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway Haloferax volcanii DSM 3757 (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?

Subunits

Subunits Comment Organism
? x * 65000, SDS-PAGE Haloferax volcanii
? x * 51975, matrix-assisted laser desorption ionization-time of flight mass spectrometry Haloferax volcanii

Synonyms

Synonyms Comment Organism
3-hydroxy-3-methylglutaryl CoA synthase
-
 Haloferax volcanii
3-hydroxy-3-methylglutaryl coenzyme A synthase
-
 Haloferax volcanii
HMGCS
-
 Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Haloferax volcanii
45
-
-
 Haloferax volcanii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 in the presence of an excess of acetyl-CoA, the half-life of the active enzyme is 27 h Haloferax volcanii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.6
-
 acetyl-CoA pH 8.0, 30°C Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Haloferax volcanii
8.5
-
-
 Haloferax volcanii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00057
-
 hymeglusin 18°C, pH 8 Haloferax volcanii

General Information

General Information Comment Organism
physiological function the enzyme is involved in the mevalonate pathway in archaea. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway Haloferax volcanii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
92
-
 acetyl-CoA pH 8.0, 30°C Haloferax volcanii