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Literature summary extracted from

  • Garau, G.; Muzzolini, L.; Tornaghi, P.; Degano, M.
    Active site plasticity revealed from the structure of the enterobacterial N-ribohydrolase RihA bound to a competitive inhibitor (2010), BMC Struct. Biol., 10, 14.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.8 RihA bound to inhibitor 3,4-diaminophenyl-D-iminoribitol, hanging drop vapour diffusion method, 8 mg/ml RihA in 50 mM HEPES, pH 7.2, 150 mM NaCl is mixed with a 5:1 molar excess of 3,4-diaminophenyl-D-iminoribitol, solubilized in 50 mM HEPES, pH 7.2, and incubated at 4°C for 3 hours, the protein/inhibitor complex is mixed with an equal volume of a precipitant solution containing 25% PEG 4000, 0.1 M sodium acetate, pH 5.0, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.8 3,4-diaminophenyl-D-iminoribitol competitive, the ligand can bind at the active site in two distinct orientations, binding structure, overview Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.2.8 Ca2+ dependent on Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.8 a pyrimidine nucleoside + H2O Escherichia coli
-
D-ribose + a pyrimidine base
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.8 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.8 a pyrimidine nucleoside + H2O
-
Escherichia coli D-ribose + a pyrimidine base
-
?
3.2.2.8 additional information catalytic cycles between the open and closed conformations of RihA, stabilization of two flexible active site regions is pivotal to establish the interactions required for substrate discrimination and catalysis, involvement of the Asp10 as general base in the mechanism, role of the conserved His82 residue in modulating product release, structure-function analysis, detailed overview Escherichia coli ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.2.8 More the enzyme belongs to the pyrimidine-preferring N-ribohydrolases, CU-NHs, a class of Ca2+-dependent enzymes that catalyze the hydrolytic cleavage of the N-glycosidic bond in pyrimidine nucleosides Escherichia coli
3.2.2.8 N-ribohydrolase
-
Escherichia coli
3.2.2.8 RihA
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.8 37
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.8 7.4
-
assay at Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.2.8 0.085
-
3,4-diaminophenyl-D-iminoribitol pH 7.4, 37°C Escherichia coli

General Information

EC Number General Information Comment Organism
3.2.2.8 physiological function possible role of CU-NHs in the breakdown of modified nucleosides derived from RNA molecules Escherichia coli