Information on EC 3.5.4.19 - phosphoribosyl-AMP cyclohydrolase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.5.4.19
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RECOMMENDED NAME
GeneOntology No.
phosphoribosyl-AMP cyclohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-C-binding
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Histidine metabolism
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L-histidine biosynthesis
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Metabolic pathways
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histidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase
The Neurospora crassa enzyme also catalyses the reactions of EC 1.1.1.23 (histidinol dehydrogenase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
CAS REGISTRY NUMBER
COMMENTARY hide
37289-22-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
Uniprot
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme catalyzes the third step of histidine biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(5-phospho-beta-D-ribosyl)-AMP + H2O
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
show the reaction diagram
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?
1-(5-phosphoribosyl)-AMP + H2O
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-(5-phosphoribosyl)-AMP + H2O
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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0.95 Cd2+ per enzyme subunit, competes with and replaces Zn2+, binding affects the enzyme structure, three Cd2+ are coordinated by residues Asp85 and Cys86 from one monomer and Cys109 from the other monomer, the fourth Cd2+ is bound by His16 and Asp89
Mg2+
required for cataltic activity. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal. The enzyme is protected from inactivation by inclusion of the substrate N1-(5'-phosphoribosyl)adenosine 5'-monophosphate, while Mg2+, a metal required for catalytic activity, enhanced the rate of inactivation
EDTA
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reversible inhibition
methyl methane thiosulfonate
compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal
Zn2+
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exogenous Zn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 10
1-(5-phospho-beta-D-ribosyl)-AMP
0.00075 - 0.0204
1-(5-phosphoribosyl)-AMP
additional information
additional information
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steady-state kinetics of the enzyme with bound Zn2+ or with Cd2+ bound at different pH, recombinant enzyme, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 9.9
1-(5-phosphoribosyl)-AMP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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dependent on bound metal ion
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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pH profile, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 65
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assays are performed at 30°C or at 65°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15486
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alpha2, 2 * 15486, MALDI-MS
31200
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ultracentrifugation
34000
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gel filtration
95000
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alpha2, 2 * 95000, SDS-PAGE
126000
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gel filtration
190000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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the cytoplasmic C-terminus harbors the active site for the histidinol dehydrogenase, EC 1.1.1.23, activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified untagged recombinant enzyme, hanging drop vapour diffusion method, 2 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed in a 1:1 ratio with reservoir solution containing 100 mM HEPES-HCl, pH 7.5, 50 mM CdSO4, 1.6 M sodium acetate, and 10% w/v glycerol, X-ray diffraction structure determination and analysis at 1.7 A resolution
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pellet by polyethylene glycol and MgCl2, stable till used
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4°C, phosphate buffer, pH 7.5, one month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by anion exchange chromatography and dialysis
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the enzyme in Escherichia coli strains MC1061 and BL21(DE3), the His-tagged enzyme constantly shows aggregation after expression
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overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C109/C116
no measurable catalytic activity, not capable of binding Zn2+
C109A
no measurable catalytic activity, not capable of binding Zn2+
C116A
no measurable catalytic activity, still capable of binding Zn2+
C93A
no measurable catalytic activity
D92E
180fold loss in catalytic efficiency (kcat/Km), decrease in Zn2+ content
D94A
no measurable catalytic activity, decrease in Zn2+ content
D94E
2300fold decrease in activity, decrease in Zn2+ content
H110A
500fold decrease in activity, no decrease in Zn2+ content
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