EC 3.5.4.25
- GTP cyclohydrolase II
IntEnz Enzyme Nomenclature
EC 3.5.4.25
Names
Accepted name:
GTP cyclohydrolase II
Other
names:
GTP-8-formylhydrolase
guanosine triphosphate cyclohydrolase II
Systematic name:
GTP 7,8-8,9-dihydrolase (formate-releasing, phosphate-releasing)
Reaction
-
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
Comments:
The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C8-N9 bond of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the α-β 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.
Links to other databases
RIB1_PICGU
RIB1_SCHPO
RIB1_YEAST
RIBA1_ARATH
RIBA1_ORYSJ
RIBA2_ORYSJ
RIBA3_ARATH
RIBA3_ORYSJ
RIBA_ACIAD
RIBA_ACIB3
RIBA_ACIB5
RIBA_ACIBC
RIBA_ACIBS
RIBA_ACIBT
RIBA_ACIBY
RIBA_ACTSZ
RIBA_AERHH
RIBA_ALIF1
RIBA_ALIFM
RIBA_ALISL
RIBA_ARCFU
RIBA_AZOBR
RIBA_AZOVD
RIBA_BAUCH
RIBA_BLOFL
RIBA_BLOPB
RIBA_BUCAI
RIBA_BUCAP
RIBA_BUCBP
RIBA_BURMA
RIBA_CAMFF
RIBA_CAMHC
RIBA_CITK8
RIBA_COLP3
RIBA_CROS8
RIBA_ECO24
RIBA_ECO27
RIBA_ECO45
RIBA_ECO55
RIBA_ECO57
RIBA_ECO5E
RIBA_ECO7I
RIBA_ECO81
RIBA_ECO8A
RIBA_ECOBW
RIBA_ECODH
RIBA_ECOHS
RIBA_ECOL5
RIBA_ECOL6
RIBA_ECOLC
RIBA_ECOLI
RIBA_ECOLU
RIBA_ECOSE
RIBA_ECOSM
RIBA_ENT38
RIBA_ESCF3
RIBA_HAEI8
RIBA_HAEIE
RIBA_HAEIG
RIBA_HAEIN
RIBA_HAES1
RIBA_HAHCH
RIBA_HAMD5
RIBA_HELAH
RIBA_HELHP
RIBA_HELP2
RIBA_HELPH
RIBA_HELPJ
RIBA_HELPS
RIBA_HELPY
RIBA_HISS2
RIBA_KLEP3
RIBA_KLEP7
RIBA_MANSM
RIBA_MARMS
RIBA_NEIG1
RIBA_NEIM0
RIBA_NEIMA
RIBA_NEIMB
RIBA_NEIMF
RIBA_PASMU
RIBA_PECAS
RIBA_PHOPO
RIBA_PICTO
RIBA_PROMH
RIBA_PSEA7
RIBA_PSEA8
RIBA_PSEAB
RIBA_PSEAE
RIBA_PSEE4
RIBA_PSEFS
RIBA_PSEP1
RIBA_PSEPG
RIBA_PSEPK
RIBA_PSEPW
RIBA_PSESM
RIBA_PSYIN
RIBA_SACD2
RIBA_SALCH
RIBA_SALPA
RIBA_SALTI
RIBA_SALTY
RIBA_SHEAM
RIBA_SHEB2
RIBA_SHEB5
RIBA_SHEB8
RIBA_SHEB9
RIBA_SHEDO
RIBA_SHEFN
RIBA_SHEHH
RIBA_SHELP
RIBA_SHEON
RIBA_SHEPA
RIBA_SHEPC
RIBA_SHEPW
RIBA_SHESA
RIBA_SHESH
RIBA_SHESM
RIBA_SHESR
RIBA_SHESW
RIBA_SHEWM
RIBA_SHIB3
RIBA_SHIBS
RIBA_SHIDS
RIBA_SHIF8
RIBA_SHIFL
RIBA_SHISS
RIBA_STRCO
RIBA_SULMU
RIBA_TERTT
RIBA_THEVO
RIBA_TOLAT
RIBA_VIBCH
RIBA_VIBPA
RIBA_VIBVU
RIBA_WIGBR
RIBA_XYLFA
RIBA_XYLFT
RIBA_YERPE
RIBA_YERPS
RIBBA_ACTP2
RIBBA_ACTP7
RIBBA_ACTPJ
RIBBA_ACTPL
RIBBA_AQUAE
RIBBA_BACAA
RIBBA_BACAC
RIBBA_BACAH
RIBBA_BACAM
RIBBA_BACAN
RIBBA_BACC0
RIBBA_BACC1
RIBBA_BACC2
RIBBA_BACC3
RIBBA_BACC4
RIBBA_BACC7
RIBBA_BACCN
RIBBA_BACCQ
RIBBA_BACCR
RIBBA_BACCZ
RIBBA_BACFN
RIBBA_BACFR
RIBBA_BACHK
RIBBA_BACMK
RIBBA_BACSK
RIBBA_BACSU
RIBBA_BACTN
RIBBA_BACVZ
RIBBA_BREBN
RIBBA_CHLL3
RIBBA_CHLMU
RIBBA_CHLPM
RIBBA_CHLPN
RIBBA_CHLTR
RIBBA_CLONN
RIBBA_CORAM
RIBBA_CORGB
RIBBA_CORGL
RIBBA_CYTH3
RIBBA_ENDTX
RIBBA_GEOSW
RIBBA_MYCA1
RIBBA_MYCA9
RIBBA_MYCBO
RIBBA_MYCBP
RIBBA_MYCBT
RIBBA_MYCGI
RIBBA_MYCMM
RIBBA_MYCPA
RIBBA_MYCTA
RIBBA_MYCTO
RIBBA_MYCTU
RIBBA_MYCUA
RIBBA_MYCVP
RIBBA_NOCFA
RIBBA_PARD8
RIBBA_PELPB
RIBBA_PHOV8
RIBBA_PORG3
RIBBA_PORGI
RIBBA_PROA2
RIBBA_RHOE4
RIBBA_RHOJR
RIBBA_SALAI
RIBBA_SALTO
RIBBA_STAAC
RIBBA_STAAM
RIBBA_STAAN
RIBBA_STAAR
RIBBA_STAAS
RIBBA_STAAW
RIBBA_STAEQ
RIBBA_STAES
RIBBA_STAHJ
RIBBA_STAS1
RIBBA_SYNWW
RIBBA_SYNY3
RIBBA_THEMA
RIBBA_THEP3
RIBBA_THEPX
RIBXA_VIBVY
References
-
Foor, F. and Brown, G.M.
Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli.
J. Biol. Chem.
250
:
3545-3551
(1975).
[PMID:
235552]
-
Smith, M. M., Beaupre, B. A., Fourozesh, D. C., Meneely, K. M., Lamb, A. L., Moran, G. R.
Finding Ways to Relax: A Revisionistic Analysis of the Chemistry of E. coli GTP Cyclohydrolase II.
Biochemistry
60
:
3027-3039
(2021).
[PMID:
34569786]
[EC 3.5.4.25 created 1984]