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Information on EC 3.5.4.10 - IMP cyclohydrolase and Organism(s) Thermotoga maritima and UniProt Accession Q9X0X6
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3.5.4.10 IMP cyclohydrolaseSpecify your search results
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- 3.5.4.10
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ecm-receptor
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The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
itga2, imp cyclohydrolase, impch, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/imp cyclohydrolase, inosine monophosphate cyclohydrolase, purh2, inosinicase, aicar transformylase/imp cyclohydrolase, mthpuro, purh2-type imp cyclohydrolase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATIC
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-
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IMP synthetase
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-
-
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IMPCHase
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-
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inosinate cyclohydrolase
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-
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inosine monophosphate cyclohydrolase
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-
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inosinicase
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
IMP 1,2-hydrolase (decyclizing)
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CAS REGISTRY NUMBER
COMMENTARY
9013-81-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-formaminoimidazole-4-carboxamide ribonucleotide
IMP + H2O
the IMPCH domain catalyzes the intramolecular cyclization of 5-formyl-AICAR, FAICAR, to IMP
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additional information
?
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the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
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-
?
additional information
?
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-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
-
-
?
additional information
?
-
-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
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-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49700
1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
20 mg/ml purified recombinant enzyme in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, nanodroplet vapor diffusion method, the crystallization solution contains 20% w/v PEG 6000 and 0.1 M citrate pH 5.0, 10% v/v PEG 200 as a cryoprotectant, X-ray diffraction structure determination and anaylsis at 1.88 A resolution, modelling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Axelrod, H.L.; McMullan, D.; Krishna, S.S.; Miller, M.D.; Elsliger, M.; Abdubek, P.; Ambing, E.; Astakhova, T.; Carlton, D.; Chiu, H.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grzechnik, S.K.; Hale, J.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Quijano, K.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon. A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 ANG. resolution
Proteins Struct. Funct. Bioinform.
71
1042-1049
2008
Thermotoga maritima (Q9X0X6), Thermotoga maritima
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