Enzymes
| UniProtKB help_outline | 1,718 proteins |
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- Name help_outline chorismate Identifier CHEBI:29748 (Beilstein: 6278304) help_outline Charge -2 Formula C10H8O6 InChIKeyhelp_outline WTFXTQVDAKGDEY-HTQZYQBOSA-L SMILEShelp_outline O[C@@H]1C=CC(=C[C@H]1OC(=C)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline prephenate Identifier CHEBI:29934 Charge -2 Formula C10H8O6 InChIKeyhelp_outline FPWMCUPFBRFMLH-XGAOUMNUSA-L SMILEShelp_outline O[C@H]1C=C[C@](CC(=O)C([O-])=O)(C=C1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13897 | RHEA:13898 | RHEA:13899 | RHEA:13900 | |
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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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Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis.
Zwahlen J., Kolappan S., Zhou R., Kisker C., Tonge P.J.
MbtI (rv2386c) from Mycobacterium tuberculosis catalyzes the initial transformation in mycobactin biosynthesis by converting chorismate to salicylate. We report here the structure of MbtI at 2.5 A resolution and demonstrate that isochorismate is a kinetically competent intermediate in the synthesi ... >> More
MbtI (rv2386c) from Mycobacterium tuberculosis catalyzes the initial transformation in mycobactin biosynthesis by converting chorismate to salicylate. We report here the structure of MbtI at 2.5 A resolution and demonstrate that isochorismate is a kinetically competent intermediate in the synthesis of salicylate from chorismate. At pH values below 7.5 isochorismate is the dominant product while above this pH value the enzyme converts chorismate to salicylate without the accumulation of isochorismate in solution. The salicylate and isochorismate synthase activities of MbtI are Mg2+-dependent, and in the absence of Mg2+ MbtI has a promiscuous chorismate mutase activity similar to that of the isochorismate pyruvate lyase, PchB, from Pseudomonas aeruginosa. MbtI is part of a larger family of chorismate-binding enzymes descended from a common ancestor (the MST family), that includes the isochorismate synthases and anthranilate synthases. The lack of active site residues unique to pyruvate eliminating members of this family, combined with the observed chorismate mutase activity, suggests that MbtI may exploit a sigmatropic pyruvate elimination mechanism similar to that proposed for PchB. Using a combination of structural, kinetic, and sequence based studies we propose a mechanism for MbtI applicable to all members of the MST enzyme family. << Less
Biochemistry 46:954-964(2007) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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THE BIOSYNTHESIS OF PHENYLALANINE AND TYROSINE; ENZYMES CONVERTING CHORISMIC ACID INTO PREPHENIC ACID AND THEIR RELATIONSHIPS TO PREPHENATE DEHYDRATASE AND PREPHENATE DEHYDROGENASE.
COTTON R.G., GIBSON F.
Biochim Biophys Acta 100:76-88(1965) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Multiple molecular forms of chorismate mutase in Bacillus subtillis.
Lorence J.H., Nester E.W.