Acetolactate decarboxylase

{{infobox enzyme

| Name = acetolactate decarboxylase

| EC_number = 4.1.1.5

| CAS_number = 9025-02-9

| GO_code = 0047605

| image =

| width =

| caption =

}}

The enzyme acetolactate decarboxylase ({{EnzExplorer|4.1.1.5}}) catalyzes the chemical reaction

:(S)-2-hydroxy-2-methyl-3-oxobutanoate $\rightleftharpoons$ (R)-2-acetoin + CO₂

Hence, this enzyme has one substrate, (S)-2-hydroxy-2-methyl-3-oxobutanoate, and two products, (R)-2-acetoin and CO₂.{{cite journal |vauthors=Hill RK, Sawada S, Arfin SM | date = 1979 | title = Stereochemistry of valine and isoleucine biosynthesis. IV Synthesis, configuration, and enzymatic specificity of alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate | journal = Bioorg. Chem. | volume = 8 | pages = 175–189 | doi = 10.1016/0045-2068(79)90003-8 | issue = 2 }}

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(R)-2-acetoin-forming]. Other names in common use include alpha-acetolactate decarboxylase, and (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase. This enzyme participates in butanoate metabolism and c5-branched dibasic acid metabolism.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code {{PDB link|1XV2}}.

References

{{cite journal | author = Stormer FC | date = 1967 | title = Isolation of crystalline pH 6 acetolactate-forming enzyme from Aerobacter aerogenes | journal = J. Biol. Chem. | volume = 242 | pages = 1756–9 | pmid = 6024768 | issue = 8 | doi = 10.1016/S0021-9258(18)96065-5 | doi-access = free }}

Category:EC 4.1.1

Category:Enzymes of known structure