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Literature summary for 3.5.4.10 extracted from

  • 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 (2008), Proteins Struct. Funct. Bioinform., 71, 1042-1049.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Thermotoga maritima

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49700
-
1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermotoga maritima 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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?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X0X6 gene TM1249 or purH
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity and anion exchange chromatography Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-formaminoimidazole-4-carboxamide ribonucleotide the IMPCH domain catalyzes the intramolecular cyclization of 5-formyl-AICAR, FAICAR, to IMP Thermotoga maritima IMP + H2O
-
?
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 Thermotoga maritima ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE Thermotoga maritima

Synonyms

Synonyms Comment Organism
AICAR transformylase/inosine 5'-monophosphate cyclohydrolase
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Thermotoga maritima
IMPCH
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Thermotoga maritima
inosine 5'-monophosphate cyclohydrolase
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Thermotoga maritima

pI Value

Organism Comment pI Value Maximum pI Value
Thermotoga maritima sequence calculation
-
5.49