Caulobacter crescentus CB15 Reaction:

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

EC Number:

Enzymes and Genes:
GTP cyclohydrolase I : folE

In Pathway: 6-hydroxymethyl-dihydropterin diphosphate biosynthesis I

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: GTP cyclohydrolase I

Enzyme Commission Synonyms: GTP cyclohydrolase, guanosine triphosphate cyclohydrolase, guanosine triphosphate 8-deformylase, dihydroneopterin triphosphate synthase, GTP 8-formylhydrolase

Enzyme Commission Summary:
The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC (sepiapterin reductase) and EC (6-pyruvoyltetrahydropterin synthase) [Supangat05].

Citations: [Wolf69, Burg68]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

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


Burg68: Burg AW, Brown GM (1968). "The biosynthesis of folic acid. 8. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate." J Biol Chem 243(9);2349-58. PMID: 4296838

Supangat05: Supangat S, Choi YK, Park YS, Son D, Han CD, Lee KH (2005). "Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum." Acta Crystallogr Sect F Struct Biol Cryst Commun 61(Pt 2);202-4. PMID: 16510994

Wolf69: Wolf WA, Brown GM (1969). "The biosynthesis of folic acid. X. Evidence for an Amadori rearrangement in the enzymatic formation of dihydroneopterin triphosphate from GTP." Biochim Biophys Acta 192(3);468-78. PMID: 4904679

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