Enzymes
| UniProtKB help_outline | 5,376 proteins |
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| GO Molecular Function help_outline |
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- Name help_outline (2S)-2-acetolactate Identifier CHEBI:58476 (Beilstein: 3604088) help_outline Charge -1 Formula C5H7O4 InChIKeyhelp_outline NMDWGEGFJUBKLB-YFKPBYRVSA-M SMILEShelp_outline CC(=O)[C@](C)(O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (R)-acetoin Identifier CHEBI:15686 (CAS: 513-86-0,53584-56-8) help_outline Charge 0 Formula C4H8O2 InChIKeyhelp_outline ROWKJAVDOGWPAT-GSVOUGTGSA-N SMILEShelp_outline C[C@@H](O)C(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 997 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21580 | RHEA:21581 | RHEA:21582 | RHEA:21583 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate decarboxylase in Streptococcus thermophilus.
Monnet C., Nardi M., Hols P., Gulea M., Corrieu G., Monnet V.
<h4>Aims</h4>To demonstrate the presence of an active alpha-acetolactate decarboxylase in Streptococcus thermophilus and to investigate its physiological function.<h4>Methods and results</h4>Streptococcus thermophilus CNRZ385 contains a gene encoding an alpha-acetolactate decarboxylase. Comparison ... >> More
<h4>Aims</h4>To demonstrate the presence of an active alpha-acetolactate decarboxylase in Streptococcus thermophilus and to investigate its physiological function.<h4>Methods and results</h4>Streptococcus thermophilus CNRZ385 contains a gene encoding an alpha-acetolactate decarboxylase. Comparison of the production of alpha-acetolactate and its decarboxylation products, by the parent strain and an alpha-acetolactate decarboxylase-deficient mutant, demonstrated the presence of a control of the pool of alpha-acetolactate by valine, leucine and isoleucine. This control occurs via an allosteric activation of the alpha-acetolactate decarboxylase. Cell-free extracts of S. thermophilus were not able to decarboxylate the isoleucine precursor alpha-acetohydroxybutyrate.<h4>Conclusions</h4>These results strongly suggest that one of the physiological functions of the alpha-acetolactate decarboxylase in S. thermophilus is to regulate leucine and valine biosynthesis by diverting the flux of alpha-acetolactate towards acetoin when the branched-chain amino acids are present at a high concentration.<h4>Significance and impact of the study</h4>Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate decarboxylase may occur in several other micro-organisms and explain some of their growth properties. << Less
Lett. Appl. Microbiol. 36:399-405(2003) [PubMed] [EuropePMC]