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Literature summary 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)

EC Number Cloned (Comment) Organism
4.1.1.71 expressed in Escherichia coli Mycolicibacterium smegmatis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.71 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.71 2-oxoglutarate Mycolicibacterium smegmatis
-
 succinate semialdehyde + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.71 Mycolicibacterium smegmatis A0R3B1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.71
-
 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.71 2-oxoglutarate
-
 Mycolicibacterium smegmatis succinate semialdehyde + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.71 alpha-ketoglutarate decarboxylase
-
 Mycolicibacterium smegmatis
4.1.1.71 E1o
-
 Mycolicibacterium smegmatis
4.1.1.71 Kgd
-
 Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.71 thiamine diphosphate
-
 Mycolicibacterium smegmatis