Literature summary for 2.3.3.10 extracted from

Steussy, C.N.; Vartia, A.A.; Burgner, J.W.; Sutherlin, A.; Rodwell, V.W.; Stauffacher, C.V.
X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA (2005), Biochemistry, 44, 14256-14267.

Search for more literature for 2.3.3.10

Crystallization (Commentary)

Crystallization (Comment)	Organism
unliganded and in complex with its second substrate/inhibitor acetoacetyl-CoA. The acetoacetyl-CoA binary structure demonstrates reduced coenzyme A and acetoacetate covalently bound to the active site cysteine through a thioester bond	Enterococcus faecalis

Inhibitors

Inhibitors	Comment	Organism	Structure
acetoacetyl-CoA	potent inhibitor of the overall reaction	Enterococcus faecalis

Organism

Organism	UniProt	Comment	Textmining
Enterococcus faecalis	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)