Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.4 In cyclic amidines
ID:3.5.4.16
Description:GTP cyclohydrolase I.
Prosite: PDOC00672;
PDB:
PDBScop
1WPL 8029414; 8041793; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8024620; 8036999;
1IS7 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793;
1IS8 8024620; 8036999; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793; 8024620; 8036999; 8024620; 8036999; 8024620; 8036999; 8029414; 8041793; 8029414; 8041793;
1FB1 8023457; 8035837; 8023457; 8035837; 8023457; 8035837; 8023457; 8035837; 8023457; 8035837;
1GTP 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783; 8023403; 8035783;
 » show all

Cath: 1.10.286.10; 3.30.1130.10; 3.30.479.10; 3.10.270.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.4.16
BRENDA Enzyme Link: BRENDA 3.5.4.16
KEGG Enzyme Link: KEGG3.5.4.16
BioCyc Enzyme Link: BioCyc 3.5.4.16
ExPASy Enzyme Link: ExPASy3.5.4.16
EC2PDB Enzyme Link: EC2PDB 3.5.4.16
ExplorEnz Enzyme Link: ExplorEnz 3.5.4.16
PRIAM enzyme-specific profiles Link: PRIAM 3.5.4.16
IntEnz Enzyme Link: IntEnz 3.5.4.16
MEDLINE Enzyme Link: MEDLINE 3.5.4.16
MSA:

3.5.4.16;

Phylogenetic Tree:

3.5.4.16;

Uniprot:
M-CSA:
RHEA:17473 GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RULE(radius=1) [OH2;+0:1].[OH;+0:2]-[CH;+0:3]1-[*:4]-[*:5]-[O;H0;+0:6]-[CH;+0:7]-1-[n;H0;+0:8]1:[*:9]:[*:10]:[n;H0;+0:11]:[cH;+0:12]:1>>[O;H0;+0:2]=[CH;+0:12]-[OH;+0:1].[OH;+0:6]-[*:5]-[*:4]-[C;H0;+0:3]1=[N;H0;+0:11]-[*:10]:[*:9]-[NH;+0:8]-[CH2;+0:7]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative.Tanaka Y, Nakagawa N, Kuramitsu S, Yokoyama S, Masui R2005 Sep16169877
Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.Rebelo J, Auerbach G, Bader G, Bracher A, Nar H, Hösl C, Schramek N, Kaiser J, Bacher A, Huber R, Fischer M2003 Feb 1412559918