Literature summary for 2.3.3.10 extracted from

Steussy, C.N.; Robison, A.D.; Tetrick, A.M.; Knight, J.T.; Rodwell, V.W.; Stauffacher, C.V.; Sutherlin, A.L.
A structural limitation on enzyme activity: the case of HMG-CoA synthase (2006), Biochemistry, 45, 14407-14414.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant A110G. Amide nitrogen of mutants S308 shifts 0.4 A toward the catalytic site cysteine residue stabilizing the intermediate negative charge. The hydroxyl group of S308 rotates to a position where it is able to stabilize the carbanion intermediate of the acetyl-S-enzyme during its condensation with acetoacetyl-CoA	Enterococcus faecalis

Protein Variants

Protein Variants	Comment	Organism
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	Enterococcus faecalis

Organism

Organism	UniProt	Comment	Textmining
Enterococcus faecalis	-	-	-

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Release 2023.1 (January 2023)