Protein Family Models

Members of this family are prephenate dehydrogenases EC:1.3.1.12 (PDHs) involved in tyrosine biosynthesis [1]. This is the C-terminal, helical dimerization domain of PDHs [1]. [1]. 31750992. Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain. Shabalin IG, Gritsunov A, Hou J, Slawek J, Miks CD, Cooper DR, Minor W, Christendat D;. FEBS J. 2020;287:2235-2255. (from Pfam)

Date:

2024-10-16

Chorismate mutase EC: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 [2,3]. [1]. 7971967. The crystal structure of allosteric chorismate mutase at 2.2-A resolution. Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G;. Proc Natl Acad Sci U S A 1994;91:10814-10818. [2]. 9642265. 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 1998;273:17012-17017. [3]. 9497350. 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 1998;273:6248-6253. (from Pfam)

Date:

2024-10-16

Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face [1]. [1]. 31750992. Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain. Shabalin IG, Gritsunov A, Hou J, Slawek J, Miks CD, Cooper DR, Minor W, Christendat D;. FEBS J. 2020;287:2235-2255. (from Pfam)

Date:

2024-10-16

This model represents the chorismate mutase domain of the gamma proteobacterial "T-protein" which consists of an N-terminal chorismate mutase domain and a C-terminal prephenate dehydrogenase domain.

Gene:

tyrA

Date:

2024-05-29

bifunctional chorismate mutase/prephenate dehydrogenase (TyrA) catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis

Date:

2018-03-05

Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis

Gene:

tyrA

Date:

2021-08-26