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Literature summary for 2.3.3.10 extracted from

  • Bock, T.; Kasten, J.; Mueller, R.; Blankenfeldt, W.
    Crystal structure of the HMG-CoA synthase MvaS from the Gram-negative bacterium Myxococcus xanthus (2016), ChemBioChem, 17, 1257-1262 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Myxococcus xanthus

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method, crystal structures of MvaS, the HMGCS from Myxococcus xanthus, in complex with CoA and acetylated active site Cys115, with the second substrate acetoacetyl CoA and with the product of the condensation reaction, 3-hydroxy-3-methylglutaryl CoA Myxococcus xanthus

General Stability

General Stability Organism
dimerization plays a role in the formation and stability of the active site Myxococcus xanthus

Organism

Organism UniProt Comment Textmining
Myxococcus xanthus Q1D4I1
-
-
Myxococcus xanthus DK 1622 Q1D4I1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Myxococcus xanthus

Synonyms

Synonyms Comment Organism
HMG-CoA synthase
-
Myxococcus xanthus
mvaS
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Myxococcus xanthus

General Information

General Information Comment Organism
metabolism in myxobacteria, the enzyme is involved in an alternative and acetyl-CoA-dependent isovaleryl CoA biosynthesis pathway Myxococcus xanthus