Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 4.1.2.50

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

EC Number: 4.1.2.50

Enzymes and Genes:
6-carboxy-5,6,7,8-tetrahydropterin synthase Inferred from experiment : queD ( Escherichia coli K-12 substr. MG1655 )
6-carboxy-5,6,7,8-tetrahydropterin synthase Inferred from experiment : queD ( Bacillus subtilis subtilis 168 )

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 Inferred by computational analysis [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].

Citations: [Cicmil08]

Gene-Reaction Schematic: ?

Unification Links: Rhea:27966

Relationship Links: BRENDA:EC:4.1.2.50 , ENZYME:EC:4.1.2.50 , IUBMB-ExplorEnz:EC:4.1.2.50

Credits:
Revised 24-Jan-2011 by Caspi R , SRI International


References

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC13A.