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Literature summary extracted from
- Structure and mechanism of acetolactate decarboxylase (2013), ACS Chem. Biol., 8, 2339-2344.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.5 | gene alsD, recombinant expression of wild-type and mutant enzymes | Bacillus subtilis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.1.5 | X-ray diffraction crystal structure determination and analysis by single wavelength anomalous dispersion method at 1.1 A resolution, ethane-1,2-diol is used as a cryoprotectant | Brevibacillus brevis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.1.5 | E251A | site-directed mutagenesis, the mutant shows highly reduced activity | Bacillus subtilis |
| 4.1.1.5 | E251Q | site-directed mutagenesis, the mutant shows highly reduced activity | Bacillus subtilis |
| 4.1.1.5 | E62A | site-directed mutagenesis, the mutant shows highly reduced activity | Bacillus subtilis |
| 4.1.1.5 | E62Q | site-directed mutagenesis, the mutant shows highly reduced activity | Bacillus subtilis |
| 4.1.1.5 | R142A | site-directed mutagenesis, the mutant shows highly reduced activity | Bacillus subtilis |
| 4.1.1.5 | R142K | site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme | Bacillus subtilis |
| 4.1.1.5 | T55A | site-directed mutagenesis, the mutant shows 2.5fold increased activity compared to the wild-type enzyme | Bacillus subtilis |
| 4.1.1.5 | T55S | site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme | Bacillus subtilis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.5 | (2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | competitive inhibition of the transition state analogue | Brevibacillus brevis |  |
| 4.1.1.5 | (2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | mixed inhibition of the transition state analogue | Brevibacillus brevis | |
| 4.1.1.5 | (2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | competitive inhibition of the transition state analogue | Brevibacillus brevis | |
| 4.1.1.5 | (2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | competitive inhibition of the transition state analogue | Brevibacillus brevis | |
| 4.1.1.5 | additional information | transition state analogues bound in the active site, structures, overview | Brevibacillus brevis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.5 | 0.49 | - |
(2S,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
| 4.1.1.5 | 0.55 | - |
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
| 4.1.1.5 | 0.56 | - |
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
| 4.1.1.5 | 0.78 | - |
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.5 | Zn2+ | ALDC is a metalloprotein with a two domain alpha/beta tertiary structure. Three highly conserved histidines 194, 196, and 207 coordinate a Zn2+ ion, together with a conserved glutamate 253 from the C-terminal tail | Brevibacillus brevis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.5 | (2S)-2-hydroxy-2-methyl-3-oxobutanoate | Bacillus subtilis | - |
(3R)-3-hydroxybutan-2-one + CO2 | - |
? | |
| 4.1.1.5 | (2S)-2-hydroxy-2-methyl-3-oxobutanoate | Brevibacillus brevis | acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that involves a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer | (3R)-3-hydroxybutan-2-one + CO2 | - |
? | |
| 4.1.1.5 | additional information | Bacillus subtilis | the enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.5 | Bacillus subtilis | - |
gene alsD | - |
| 4.1.1.5 | Brevibacillus brevis | P23616 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.1.1.5 | (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2 | catalytic decarboxylation mechanism, overview | Brevibacillus brevis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.5 | (2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | transition state analogue acts as substrate and competitive inhibitor | Brevibacillus brevis | ? | - |
? | |
| 4.1.1.5 | (2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | transition state analogue acts as substrate and mixed-type inhibitor | Brevibacillus brevis | ? | - |
? | |
| 4.1.1.5 | (2S)-2-hydroxy-2-methyl-3-oxobutanoate | - |
Bacillus subtilis | (3R)-3-hydroxybutan-2-one + CO2 | - |
? | |
| 4.1.1.5 | (2S)-2-hydroxy-2-methyl-3-oxobutanoate | acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that involves a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer | Brevibacillus brevis | (3R)-3-hydroxybutan-2-one + CO2 | - |
? | |
| 4.1.1.5 | (2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | transition state analogue acts as substrate and competitive inhibitor | Brevibacillus brevis | ? | - |
? | |
| 4.1.1.5 | (2S,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | transition state analogue acts as substrate and competitive inhibitor | Brevibacillus brevis | ? | - |
? | |
| 4.1.1.5 | (2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | transition state analogue acts as substrate and competitive inhibitor | Brevibacillus brevis | ? | - |
? | |
| 4.1.1.5 | additional information | the enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one | Bacillus subtilis | ? | - |
? | |
| 4.1.1.5 | additional information | the enzyme appears to catalyze both the stereoselective decarboxylation/protonation and the rearrangement reaction of the non-natural substrate. The enzyme isomerizes (S)-2-acetohydroxybutyrate to (R)-3-hydroxypentan-2-one and (S)-2-hydroxy-2-methyl-3-oxopentanoate to (R)-2-hydroxypentan-3-one | Brevibacillus brevis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.1.5 | More | ALDC is a metalloprotein with a two domain alpha/beta tertiary structure. The N-terminal domain comprises a 7-stranded mixed beta-sheet that extends into the equivalent beta-sheet of the 2-fold symmetry-related molecule generating a 14-stranded beta-sheet that spans the physiologically relevant dimeric assembly | Brevibacillus brevis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.5 | ALDC | - |
Bacillus subtilis |
| 4.1.1.5 | ALDC | - |
Brevibacillus brevis |
| 4.1.1.5 | AlsD | - |
Bacillus subtilis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.5 | 6 | - |
assay at | Brevibacillus brevis |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.5 | 0.46 | - |
(2S,3S)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
| 4.1.1.5 | 0.76 | - |
(2R,3R)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
| 4.1.1.5 | 1.72 | - |
(2S,3R)-[(2S)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
| 4.1.1.5 | 7.68 | - |
(2R,3S)-[(2R)-3-hydroxy-2-(hydroxy-kappaO)-2-methylbutanoic acid-kappaO]zinc(2+) | pH 6.0, temperature not specified in the publication | Brevibacillus brevis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.1.5 | additional information | ALDC does not contain a basic lysine residue capable of forming an imine intermediate prior to decarboxylation | Brevibacillus brevis |
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