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Literature summary for 5.1.99.1 extracted from

  • McCarthy, A.A.; Baker, H.M.; Shewry, S.C.; Patchett, M.L.; Baker, E.N.
    Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold (2001), Structure, 9, 637-646.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of native, Co2+-substituted and SeMet-substituted enzyme by hanging-drop vapour-diffusion method Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

Metals/Ions Comment Organism Structure
additional information His12, Gln65, His91 and Glu141 provide a binding site for a divalent metal ion, as shown by binding of Co2+ Propionibacterium freudenreichii subsp. shermanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Propionibacterium freudenreichii subsp. shermanii essential enzyme in the breakdown of odd-numbered fatty acids and of the amino acids valine, isoleucine, and methionine ?
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Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii subsp. shermanii
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-methylmalonyl-CoA
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Propionibacterium freudenreichii subsp. shermanii (S)-methylmalonyl-CoA
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?
additional information essential enzyme in the breakdown of odd-numbered fatty acids and of the amino acids valine, isoleucine, and methionine Propionibacterium freudenreichii subsp. shermanii ?
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?

Synonyms

Synonyms Comment Organism
MMCE
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Propionibacterium freudenreichii subsp. shermanii