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- Name help_outline (R)-carnitinyl-CoA Identifier CHEBI:60932 Charge -3 Formula C28H46N8O18P3S InChIKeyhelp_outline BBRISSLDTUHWKG-PVMHLSDZSA-K SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C[C@@H](O)C[N+](C)(C)C 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 crotonobetainyl-CoA Identifier CHEBI:60933 Charge -3 Formula C28H44N8O17P3S InChIKeyhelp_outline WAUPBDVHJXXZGW-HXPULJKESA-K SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)\C=C\C[N+](C)(C)C 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:28338 | RHEA:28339 | RHEA:28340 | RHEA:28341 | |
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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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Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp.
Engemann C., Elssner T., Pfeifer S., Krumbholz C., Maier T., Kleber H.P.
Enzymes involved in carnitine metabolism of Proteus sp. are encoded by the cai genes organised as the caiTABCDEF operon. The complete operon could be sequenced from the genomic DNA of Proteus sp. Amino acid sequence similarities and/or enzymatic analysis confirmed the function assigned to each pro ... >> More
Enzymes involved in carnitine metabolism of Proteus sp. are encoded by the cai genes organised as the caiTABCDEF operon. The complete operon could be sequenced from the genomic DNA of Proteus sp. Amino acid sequence similarities and/or enzymatic analysis confirmed the function assigned to each protein involved in carnitine metabolism. CaiT was suggested to be an integral membrane protein responsible for the transport of betaines. The caiA gene product was shown to be a crotonobetainyl-CoA reductase catalysing the irreversible reduction of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA. CaiB and CaiD were identified to be the two components of the crotonobetaine hydrating system, already described. CaiB and caiD were cloned and expressed in Escherichia coli. After purification of both proteins, their individual enzymatic functions were solved. CaiB acts as betainyl-CoA transferase specific for carnitine, crotonobetaine, gamma-butyrobetaine and its CoA derivatives. Transferase reaction proceeds, following a sequential bisubstrate mechanism. CaiD was identified to be a crotonobetainyl-CoA hydratase belonging to the crotononase superfamily. Because of amino acid sequence similarities, CaiC was suggested to be a betainyl-CoA ligase. Taken together, these results show that the metabolism of carnitine and crotonobetaine in Proteus sp. proceeds at the CoA level. << Less
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Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.
Engemann C., Elssner T., Kleber H.-P.
Two proteins, component I (CI) and component II (CII), catalyze the biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp. CI was purified to electrophoretic homogeneity from cell-free extracts of Proteus sp. The N-terminal amino acid sequence of CI showed high similarity (80%) to th ... >> More
Two proteins, component I (CI) and component II (CII), catalyze the biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp. CI was purified to electrophoretic homogeneity from cell-free extracts of Proteus sp. The N-terminal amino acid sequence of CI showed high similarity (80%) to the caiB gene product from Escherichia coli O44K74, which encodes the L(-)-carnitine dehydratase. CI alone was unable to convert crotonobetaine into L(-)-carnitine even in the presence of the cosubstrates crotonobetainyl-CoA or gamma-butyrobetainyl-CoA, which are essential for this biotransformation. The relative molecular mass of CI was determined to be 91.1 kDa. CI is composed of two identical subunits of molecular mass 43.6 kDa. The isoelectric point is 5.0. CII was purified to electrophoretic homogeneity from cell-free extracts of Proteus sp. and its N-terminal amino acid sequence showed high similarity (75%) to the caiD gene product of E. coli O44K74. The relative molecular mass of CII was shown to be 88.0 kDa, and CII is composed of three identical subunits of molecular mass 30.1 kDa. The isoelectric point of CII is 4.9. For the biotransformation of crotonobetaine to L(-)-carnitine, the presence of CI, CII, and a cosubstrate (crotonobetainyl-CoA or gamma-butyrobetainyl-CoA) were shown to be essential. << Less
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Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli.
Elssner T., Engemann C., Baumgart K., Kleber H.-P.
Two proteins (CaiB and CaiD) were found to catalyze the reversible biotransformation of crotonobetaine to L-carnitine in Escherichia coli in the presence of a cosubstrate (e.g., gamma-butyrobetainyl-CoA or crotonobetainyl-CoA). CaiB (45 kDa) and CaiD (27 kDa) were purified in two steps to electrop ... >> More
Two proteins (CaiB and CaiD) were found to catalyze the reversible biotransformation of crotonobetaine to L-carnitine in Escherichia coli in the presence of a cosubstrate (e.g., gamma-butyrobetainyl-CoA or crotonobetainyl-CoA). CaiB (45 kDa) and CaiD (27 kDa) were purified in two steps to electrophoretic homogeneity from overexpression strains. CaiB was identified as crotonobetainyl-CoA:carnitine CoA-transferase by MALDI-TOF mass spectrometry and enzymatic assays. The enzyme exhibits high cosubstrate specificity to CoA derivatives of trimethylammonium compounds. In particular, the N-terminus of CaiB shows significant identity with other CoA-transferases (e.g., FldA from Clostridium sporogenes, Frc from Oxalobacter formigenes, and BbsE from Thauera aromatica) and CoA-hydrolases (e.g., BaiF from Eubacterium sp.). CaiD was shown to be a crotonobetainyl-CoA hydratase using MALDI-TOF mass spectrometry and enzymatic assays. Besides crotonobetainyl-CoA CaiD is also able to hydrate crotonyl-CoA with a significantly lower Vmax (factor of 10(3)) but not crotonobetaine. The substrate specificity of CaiD and its homology to the crotonase confirm this enzyme as a new member of the crotonase superfamily. Concluding these results, it was verified that hydration of crotonobetaine to L-carnitine proceeds at the CoA level in two steps: the CaiD catalyzed hydration of crotonobetainyl-CoA to L-carnitinyl-CoA, followed by a CoA transfer from L-carnitinyl-CoA to crotonobetaine, catalyzed by CaiB. When gamma-butyrobetainyl-CoA was used as a cosubstrate (CoA donor), the first reaction is the CoA transfer. The optimal ratios of CaiB and CaiD during this hydration reaction, determined to be 4:1 when crotonobetainyl-CoA was used as cosubstrate and 5:1 when gamma-butyrobetainyl-CoA was used as cosubstrate, are different from that found for in vivo conditions (1:3). << Less
Biochemistry 40:11140-11148(2001) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.