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2.3.3.14: homocitrate synthase

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

Word Map on EC 2.3.3.14

Reaction

acetyl-CoA
+
H2O
 +
2-oxoglutarate
=
(2R)-2-hydroxybutane-1,2,4-tricarboxylate
 +
CoA

Synonyms

2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating), acetyl-coenzyme A: 2-ketoglutarate C-transferase, acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, EC 4.1.3.21, HCS, HcsA, homocitrate synthase, homocitrate synthetase, homocitrate-condensing enzyme, homocondensing enzyme, LYS20, LYS21, Lys21p, LYS22, Lys22p, nifV, nifV2, saci_1304, SpHCS, synthase, homocitrate, TtHCS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.14 homocitrate synthase

Engineering

Engineering on EC 2.3.3.14 - homocitrate synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E155A
-
mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. Activity of E155A can be partially rescued by formate
E155Q
-
mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. The kcat for E155Q decreases at high pH, similar to the wild-type enzyme, but is pH independent at low pH
H309A
-
inactive mutant enzyme. Slight increase in activity is observed for H309A in the presence of 300 mM imidazole, which is still 1000fold lower than that of wild type
H309N
-
inactive mutant enzyme
Y320F
-
mutant enzyme loses 25fold activity compared to that of the wild-type enzyme
E167A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
E167Q
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
E74A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
E74Q
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
H103A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
Q47A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
R163A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
R163K
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
R163Q
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
R43A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
R43K
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
R43Q
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
S165A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
T197A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
T197S
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
T197V
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
Y332A
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
Y332F
-
mutant, reveals the contribution of this residue to substrate binding and catalysis
H72L
-
replacement of His72 by leucine makes HCS resistant to lysine inhibition, demonstrating the regulatory role of this conserved residue
additional information