Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.4.25 - GTP cyclohydrolase II and Organism(s) Pseudomonas%20aeruginosa

for references in articles please use BRENDA:EC3.5.4.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the alpha-beta phosphodiester bond of the triphosphate to form diphosphate. The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions. The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively. It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, GTP cyclohydrolase I, EC 3.5.4.29, GTP cyclohydrolase IIa, and EC 3.5.4.39, GTP cyclohydrolase IV.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas%20aeruginosa
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in selected viruses and cellular organisms
Synonyms
gtp cyclohydrolase ii, riba2, 3,4-dihydroxy-2-butanone 4-phosphate synthase, gchii, gch ii, gtp cyclohydrolase 2, gch-ii, nbriba, gtp cyclohydrolase-ii, guanosine triphosphate cyclohydrolase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GTP 7,8-8,9-dihydrolase (diphosphate-forming)
-
-
-
-
GTP-8-formylhydrolase
-
-
-
-
guanosine triphosphate cyclohydrolase II
-
-
-
-
ribA
-
-
-
-
RIBIV
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bonds
-
-
-
-
hydrolysis of phosphoesters
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP 7,8-8,9-dihydrolase (formate-releasing, phosphate-releasing)
The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the alpha-beta phosphodiester bond of the triphosphate to form diphosphate. The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions. The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively. It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, GTP cyclohydrolase I, EC 3.5.4.29, GTP cyclohydrolase IIa, and EC 3.5.4.39, GTP cyclohydrolase IV.
CAS REGISTRY NUMBER
COMMENTARY hide
56214-35-8
-