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2.3.3.10: hydroxymethylglutaryl-CoA synthase

This is an abbreviated version!
For detailed information about hydroxymethylglutaryl-CoA synthase, go to the full flat file.

Word Map on EC 2.3.3.10

Reaction

acetyl-CoA
+
H2O
 +
acetoacetyl-CoA
=
(S)-3-hydroxy-3-methylglutaryl-CoA
 +
CoA

Synonyms

(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating), 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase, 3-hydroxy-3-methylglutaryl CoA synthase, 3-hydroxy-3-methylglutaryl CoA synthase I, 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-CoA synthase 1, 3-hydroxy-3-methylglutaryl-CoA synthase 2, 3-hydroxy-3-methylglutaryl-coenzyme A synthase, 3-hydroxy-3-methylglutaryl_coenzyme A synthase, 3-hydroxyl-3-methyl-glutaryl-CoA synthase, acetoacetyl coenzyme A transacetase, beta-hydroxy-beta-methylglutaryl-CoA synthase, BjHMGS1, BjHMGS2, BjHMGS3, BjHMGS4, EC 4.1.3.5, GbHMGS2, GhHMGS1A, GhHMGS1D, GhHMGS2D, GhHMGS3A, GhHMGS3D, HGMS, HMG-CoA, HMG-CoA synthase, HMG-CoA synthase 1, HMG-CoS synthase, HMGCS, HMGCS1, HMGCS2, HMGS, HMGS-2, HMGS1, HMGS2, hydroxy-methylglutaryl coenzyme-A synthase, hydroxymethylglutaryl CoA synthase 2, hydroxymethylglutaryl CoA synthetase, hydroxymethylglutaryl coenzyme A synthase, hydroxymethylglutaryl coenzyme A-condensing enzyme, hydroxymethylglutaryl-CoA synthase, hydroxymethylglutaryl-coenzyme A synthase, LcHMGS, mvaS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.10 hydroxymethylglutaryl-CoA synthase

Engineering

Engineering on EC 2.3.3.10 - hydroxymethylglutaryl-CoA synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C212C
-
mutation causes 6fold decreased maximal velocity
H188N
H188N/S359A
N115A
-
KI value for acetoacetyl-CoA is 2.3fold higher than the wild-type value, the turnover number for acetyl-CoA is 17.7fold lower than wild-type value, KM-value is 1.6fold lower than wild-type value
R157A
-
mutation causes 14fold decreased maximal velocity
S356A
-
KI value for acetoacetyl-CoA is 5.2fold higher than the wild-type value, the turnover number for acetyl-CoA is 25.8fold lower than wild-type value, KM-value is 1.6fold lower than wild-type value
S359A
S89A
-
KI value for acetoacetyl-CoA is 1.2fold higher than the wild-type value, the turnover number for acetyl-CoA is 54.6fold lower than wild-type value, KM-value is 2.3fold lower than wild-type value
H189Q
the mutation disrupts enzyme function and diminishes cholesterol synthesis
A110G
-
overall reaction rate increases 140fold due to adjustments in the active site that result in additional stabilization of all three steps of the reaction pathway. Crystallization data
C117A
-
Km-value for acetyl-CoA is 1.7fold higher than the wild-type value, specific activity is 30% of wild-type activity
N326A
-
Km-value for acetyl-CoA is 1.6fold higher than the wild-type value, specific activity is 5% of wild-type activity
F174L
the mutant shows 10000fold decrease of activity compared to the wild type enzyme
G169D
the mutant is associated with HMGCS2 deficiency
G212R
inactive
G388R
the mutant is associated with HMGCS2 deficiency
I407T
the mutant is associated with HMGCS2 deficiency
I56N
the mutant is associated with HMGCS2 deficiency
K243E
the mutant is associated with HMGCS2 deficiency
L266S
the mutant is associated with HMGCS2 deficiency
M307T
the mutant is associated with HMGCS2 deficiency
R188H
the mutant is associated with HMGCS2 deficiency
R424X
the truncated mutant is nonfunctional
R500H
inactive
R505Q
the mutant is associated with HMGCS2 deficiency
T233A
the mutant is associated with HMGCS2 deficiency
V54M
the mutant is associated with HMGCS2 deficiency
Y167C
the mutant is associated with HMGCS2 deficiency
Y84X
the truncated mutant is nonfunctional
additional information
-
construction of a double mutant by deletion of genes involved in leucine degradation and disruption of hydroxymethylglutaryl-Coa synthase gene. For the mutant, a dramatic decrease is observed of isovaleryl-CoA derived iso-odd fatty acids