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Literature summary for 3.5.4.16 extracted from

  • Higgins, C.E.; Gross, S.S.
    The N-terminal peptide of mammalian GTP cyclohydrolase I is an autoinhibitory control element and contributes to binding the allosteric regulatory protein GFRP (2011), J. Biol. Chem., 286, 11919-11928.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.4.16

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type GTPCH as maltose-binding protein fusion protein in Escherichia coli, expression of a His-tagged GTPCH truncation mutant, devoid of 45 N-terminal amino acids, DELTA45-GTPCH, in HEK-293 cells Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
GTPCH feedback regulatory protein GFRP, the allosteric regulatory protein GFRP triggers a noncompetitive attenuation of GTPCH activity, an allosteric effector is unnecessary for GFRP to influence GTPCH activity. GFRP-mediated allosteric regulation by small molecule effectors is indistinguishable for truncated mutant DELTA45-GTPCH and wild-type GTPCH Rattus norvegicus
additional information the N-terminal peptide of mammalian GTP cyclohydrolase I is an autoinhibitory control element and contributes to binding the allosteric regulatory protein GFRP. The autoinhibitory peptide provides a molecular mechanism for physiological up-regulation of GTPCH activity Rattus norvegicus
tetrahydrobiopterin BH4, can limit its own synthesis by triggering decameric GTPCH to assemble in an inhibitory complex with two GTPCH feedback regulatory protein, GFRP, pentamers Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0179
-
 GTP pH 7.8, 37°C, wild-type enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type GTPCH maltose-binding protein fusion protein from Escherichia coli by amylose affinity chromatography and cleavage of the fusion tag by TEV protease, purification of His-tagged DELTA45-GTPCH mutant from HEK-293 cells by metal affinity chromatography Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Rattus norvegicus formate + 7,8-dihydroneopterin 3'-triphosphate
-
 ?

Subunits

Subunits Comment Organism
decamer
-
 Rattus norvegicus
More multimeric assemblies of wild-type GTPCH and truncation mutant DELTA45-GTPCH on their own display markedly different banding patterns Rattus norvegicus

Synonyms

Synonyms Comment Organism
GTPCH
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Rattus norvegicus

Expression

Organism Comment Expression
Rattus norvegicus the autoinhibitory peptide provides a molecular mechanism for physiological up-regulation of GTPCH activity up

General Information

General Information Comment Organism
malfunction multimeric assemblies of wild-type GTPCH and truncation mutant DELTA45-GTPCH on their own display markedly different banding patterns Rattus norvegicus
metabolism the N-terminal peptide of mammalian GTP cyclohydrolase I is an autoinhibitory control element and contributes to binding the allosteric regulatory protein GFRP Rattus norvegicus
physiological function the autoinhibitory peptide provides a molecular mechanism for physiological up-regulation of GTPCH activity. GTPCH activity regulation by GTPCH feedback regulatory protein, GFRP Rattus norvegicus