Literature summary for 3.5.4.29 extracted from

Morrison, S.D.; Roberts, S.A.; Zegeer, A.M.; Montfort, W.R., Bandarian, V.
A new use for a familiar fold: the X-ray crystal structure of GTP-bound GTP cyclohydrolase III from Methanocaldococcus jannaschii reveals a two metal ion catalytic mechanism (2007), Biochemistry, 47, 230-242.

Search for more literature for 3.5.4.29

Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed in Escheriochia coli	Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment)	Organism
large square orthorhombic crystals containing the enzyme/GTP complex are obtained when both GTP and K+ is present in the crystallization drop and when Mg2+ is absent	Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	calcium is detected up to 10fold in molar excess of the protein. Treatment of the protein with Chelex (Na+ form) reduces the Ca2+ to 4fold excess but does not eliminate it	Methanocaldococcus jannaschii
K+	activates	Methanocaldococcus jannaschii
Mg2+	required	Methanocaldococcus jannaschii
additional information	three metal ions are located in the active site, two of which occupy positions that are analogous to those occupied by divalent metal ions in the structures of a number of palm domain containing proteins, such as DNA polymerase I. Two conserved Asp residues that coordinate the metal ions, which are also found in palm domain containing proteins, are observed in GCH III. Site-directed variants (Asp->Asn) of these residues in GCH III are less active than wild-type. The third metal ion, most likely a potassium ion, is involved in substrate recognition through coordination of O6 of GTP. The arrangement of the metal ions in the active site suggests that GCH III utilizes two metal ion catalysis	Methanocaldococcus jannaschii
NH4+	activates	Methanocaldococcus jannaschii

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	Q57609	-	-
Methanocaldococcus jannaschii DSM 2661	Q57609	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + 3 H2O	-	Methanocaldococcus jannaschii	2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + 2 phosphate	-	?
GTP + 3 H2O	-	Methanocaldococcus jannaschii DSM 2661	2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + 2 phosphate	-	?

Subunits

Subunits	Comment	Organism
homotetramer	each monomer is composed of an N- and a C-terminal domain that adopt nearly superimposible structures, suggesting that the protein has arisen by gene duplication	Methanocaldococcus jannaschii

Synonyms

Synonyms	Comment	Organism
GCH III	-	Methanocaldococcus jannaschii
GTP cyclohydrolase III	-	Methanocaldococcus jannaschii
MJ0145	locus name	Methanocaldococcus jannaschii

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)