IPR036979
Chorismate mutase domain superfamily
InterPro entry
Short name | CM_dom_sf |
Overlapping entries |
Description
Chorismate mutase (
5.4.99.5) catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine
[2, 1]. Prephenate dehydratase (
IPR001086,
4.2.1.51, PDT) catalyses the decarboxylation of prephenate into phenylpyruvate. In microorganisms PDT is involved in the terminal pathway of the biosynthesis of phenylalanine. In some bacteria, such as Escherichia coli, PDT is part of a bifunctional enzyme (P-protein) that also catalyzes the transformation of chorismate into prephenate (chorismate mutase) while in other bacteria it is a monofunctional enzyme. The sequence of monofunctional chorismate mutase aligns well with the N-terminal part of P-proteins
[2].
References
1.Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B. J. Biol. Chem. 273, 6248-53, (1998). View articlePMID: 9497350
2.Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. Schnappauf G, Krappmann S, Braus GH. J. Biol. Chem. 273, 17012-7, (1998). View articlePMID: 9642265
GO terms
biological process
molecular function
- None
cellular component
- None
Cross References
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:1.20.59.10
Representative structure
5hub: High-resolution structure of chorismate mutase from Corynebacterium glutamicum