|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
Enzymes and Genes:
|Bacillus subtilis subtilis 168 :||6-carboxy-5,6,7,8-tetrahydropterin synthase
|Escherichia coli K-12 substr. MG1655 :||6-carboxy-5,6,7,8-tetrahydropterin synthase
In Pathway: preQ0 biosynthesis
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 6-carboxytetrahydropterin synthase
Enzyme Commission Synonyms: CPH4 synthase, queD (gene name), ToyB, ykvK (gene name)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -4.5476685 [Latendresse13]
Enzyme Commission Summary:
Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine. The enzyme from Escherichia coli can also convert 6-pyruvoyl tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin [McCarty09].
Unification Links: Rhea:27966
Cicmil08: Cicmil N, Shi L (2008). "Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis." Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 2);119-22. PMID: 18259064
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493