Category:Complex:CHORISMUTPREPHENDEHYDROG-CPLX
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Comments (originally from EcoCyc[1][2]) This enzyme catalyzes the first and second steps in the biosynthesis of tyrosine. The enzyme occurs in two aggregation states, a dimer and a tetramer. The tetrameric species is only observed in the presence of the co-factor NAD+ and/or the end product inhibitor tyrosine. [3][4][4]
References
- ↑ EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Hudson, GS et al. (1983) The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model. J. Biol. Chem. 258 3114-20 PubMed
- ↑ 4.0 4.1 Hudson, GS et al. (1984) Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine. Biochemistry 23 6240-9 PubMed
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