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Literature summary for 4.1.1.5 extracted from

  • Zhao, C.; Su, H.; Liu, Y.
    Catalytic mechanism of acetolactate decarboxylase from Brevibacillus brevis towards both enantiomers of alpha-acetolactate (2016), RSC Adv., 6, 80621-80629 .
No PubMed abstract available
Search for more literature for 4.1.1.5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2S)-2-hydroxy-2-methyl-3-oxobutanoate Brevibacillus brevis
-
 (3R)-3-hydroxybutan-2-one + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R)-2-hydroxy-2-methyl-3-oxobutanoate
-
 Brevibacillus brevis (3R)-3-hydroxybutan-2-one + CO2
-
 ?
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
-
 Brevibacillus brevis (3R)-3-hydroxybutan-2-one + CO2
-
 ?

Synonyms

Synonyms Comment Organism
ALDC
-
 Brevibacillus brevis