Literature summary for 3.5.4.16 extracted from

Funderburk, C.D.; Bowling, K.M.; Xu, D.; Huang, Z.; ODonnell, J.M.
A typical N-terminal extensions confer novel regulatory properties on GTP cyclohydrolase isoforms in Drosophila melanogaster (2006), J. Biol. Chem., 281, 33302-33312.

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Protein Variants

Protein Variants	Comment	Organism
S37E	the enzymatic activity is significantly higher than of wild type GTPCH isoform C	Drosophila melanogaster

Inhibitors

Inhibitors	Comment	Organism	Structure
DAHP	non-competitive inhibitor	Drosophila melanogaster

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
39000	-	isoform A, SDS-PAGE	Drosophila melanogaster
45000	-	isoform B, SDS-PAGE	Drosophila melanogaster
47000	-	isoform C, SDS-PAGE	Drosophila melanogaster

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA resin column chromatography	Drosophila melanogaster

Source Tissue

Source Tissue	Comment	Organism	Textmining
embryo	-	Drosophila melanogaster	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Drosophila melanogaster	formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate	-	?

Synonyms

Synonyms	Comment	Organism
GTPCHI	-	Drosophila melanogaster

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Release 2023.1 (January 2023)