Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:
6-carboxy-5,6,7,8-tetrahydropterin synthase Inferred from experiment : queD

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)

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].

Citations: [Cicmil08]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC:


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

McCarty09: McCarty RM, Somogyi A, Bandarian V (2009). "Escherichia coli QueD Is a 6-Carboxy-5,6,7,8-tetrahydropterin Synthase (dagger)." Biochemistry 48(11);2301-3. PMID: 19231875

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Oct 6, 2015, biocyc14.