Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline L-cysteine Identifier CHEBI:35235 Charge 0 Formula C3H7NO2S InChIKeyhelp_outline XUJNEKJLAYXESH-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CS)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 61 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O-acetyl-L-homoserine Identifier CHEBI:57716 Charge 0 Formula C6H11NO4 InChIKeyhelp_outline FCXZBWSIAGGPCB-YFKPBYRVSA-N SMILEShelp_outline CC(=O)OCC[C@H]([NH3+])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 acetate Identifier CHEBI:30089 (Beilstein: 1901470; CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 174 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 L,L-cystathionine Identifier CHEBI:58161 Charge 0 Formula C7H14N2O4S InChIKeyhelp_outline ILRYLPWNYFXEMH-WHFBIAKZSA-N SMILEShelp_outline [NH3+][C@@H](CCSC[C@H]([NH3+])C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:30931 | RHEA:30932 | RHEA:30933 | RHEA:30934 | |
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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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The metIC operon involved in methionine biosynthesis in Bacillus subtilis is controlled by transcription antitermination.
Auger S., Yuen W.H., Danchin A., Martin-Verstraete I.
There are two major pathways for methionine biosynthesis in micro-organisms. Little is known about these pathways in Bacillus subtilis. The authors assigned a function to the metI (formerly yjcI) and metC (formerly yjcJ) genes of B. subtilis by complementing Escherichia coli metB and metC mutants, ... >> More
There are two major pathways for methionine biosynthesis in micro-organisms. Little is known about these pathways in Bacillus subtilis. The authors assigned a function to the metI (formerly yjcI) and metC (formerly yjcJ) genes of B. subtilis by complementing Escherichia coli metB and metC mutants, analysing the phenotype of B. subtilis metI and metC mutants, and carrying out enzyme activity assays. These genes encode polypeptides belonging to the cystathionine gamma-synthase family of proteins. Interestingly, the MetI protein has both cystathionine gamma-synthase and O-acetylhomoserine thiolyase activities, whereas the MetC protein is a cystathionine beta-lyase. In B. subtilis, the transsulfuration and the thiolation pathways are functional in vivo. Due to its dual activity, the MetI protein participates in both pathways. The metI and metC genes form an operon, the expression of which is subject to sulfur-dependent regulation. When the sulfur source is sulfate or cysteine the transcription of this operon is high. Conversely, when the sulfur source is methionine its transcription is low. An S-box sequence, which is located upstream of the metI gene, is involved in the regulation of the metIC operon. Northern blot experiments demonstrated the existence of two transcripts: a small transcript corresponding to the premature transcription termination at the terminator present in the S-box and a large one corresponding to transcription of the complete metIC operon. When methionine levels were limiting, the amount of the full-length transcript increased. These results substantiate a model of regulation by transcription antitermination. << Less
Microbiology 148:507-518(2002) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.