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Literature summary for 4.1.1.71 extracted from

  • Wagner, T.; Barilone, N.; Alzari, P.M.; Bellinzoni, M.
    A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (alpha-ketoglutarate decarboxylase) (2014), Biochem. J., 457, 425-434.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Mycolicibacterium smegmatis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 52-59% (w/v) 2-methyl-2,4-pentanediol and 22-25 mM sodium acetate Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate Mycolicibacterium smegmatis
-
succinate semialdehyde + CO2
-
?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0R3B1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate
-
Mycolicibacterium smegmatis succinate semialdehyde + CO2
-
?

Synonyms

Synonyms Comment Organism
alpha-ketoglutarate decarboxylase
-
Mycolicibacterium smegmatis
E1o
-
Mycolicibacterium smegmatis
Kgd
-
Mycolicibacterium smegmatis

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Mycolicibacterium smegmatis