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Literature summary extracted from

  • Preumont, A.; Snoussi, K.; Stroobant, V.; Collet, J.F.; Van Schaftingen, E.
    Molecular identification of pseudouridine-metabolizing enzymes (2008), J. Biol. Chem., 283, 25238-25246.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.83
-
Escherichia coli
4.2.1.70 expression as His-tagged enzyme in Escherichia coli Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.83 additional information mutants lacking YeiC activity are unable to metabolize pseudouridine Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.70 Ni2+
-
Escherichia coli
4.2.1.70 Zn2+
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.83 0.12
-
pseudouridine pH 7.1, 30°C Escherichia coli
2.7.1.83 0.33
-
ATP pH 7.1, 30°C Escherichia coli
4.2.1.70 0.06
-
pseudouridine 5'-phosphate pH 7.1, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.83 Mg2+ required Escherichia coli
2.7.1.83 Mg2+ enzyme is dependent on the presence of Mg2+ Escherichia coli
4.2.1.70 Co2+ high activity Escherichia coli
4.2.1.70 Fe2+ high activity Escherichia coli
4.2.1.70 Mn2+ high activity Escherichia coli
4.2.1.70 additional information YeiN is dependent on divalent cations Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.83 ATP + pseudouridine Escherichia coli two enzymes are involved in the metabolism of pseudouridine in uropathogenic Escherichia coli, the principal agent of urinary tract infections in humans. The first enzyme, coded by the gene yeiC, specifically phosphorylates pseudouridine to pseudouridine 5'-phosphate. yeiC- mutants are unable to metabolize pseudouridine, in contrast to wild-type Escherichia coli UTI89. The second enzyme, encoded by the gene yeiN (EC 4.2.1.70) belonging to the same operon as yeiC, catalyzes the conversion of pseudouridine 5'-phosphate to uracil and ribose 5-phosphate in a divalent cation-dependent manner ADP + pseudouridine 5'-phosphate
-
?
4.2.1.70 uracil + D-ribose 5-phosphate Thermotoga maritima the association of IndA with pseudouridine kinase indicates that it serves physiologically to metabolize pseudouridine 5'-phosphate rather than to form it pseudouridine 5'-phosphate + H2O
-
r
4.2.1.70 uracil + D-ribose 5-phosphate Escherichia coli the enzyme is involved in the metabolism of pseudouridine in uropathogenic Escherichia coli pseudouridine 5'-phosphate + H2O
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.83 Escherichia coli
-
-
-
2.7.1.83 Escherichia coli P30235 strain UTI89
-
4.2.1.70 Escherichia coli P33025 gene yeiN
-
4.2.1.70 Thermotoga maritima
-
gene indA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.83
-
Escherichia coli
4.2.1.70
-
Thermotoga maritima
4.2.1.70 recombinant His-tagged enzyme from Escherichia coli by affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.83 ATP + pseudouridine
-
Escherichia coli ADP + pseudouridine 5'-monophosphate
-
?
2.7.1.83 ATP + pseudouridine
-
Escherichia coli ADP + pseudouridine 5'-phosphate
-
?
2.7.1.83 ATP + pseudouridine two enzymes are involved in the metabolism of pseudouridine in uropathogenic Escherichia coli, the principal agent of urinary tract infections in humans. The first enzyme, coded by the gene yeiC, specifically phosphorylates pseudouridine to pseudouridine 5'-phosphate. yeiC- mutants are unable to metabolize pseudouridine, in contrast to wild-type Escherichia coli UTI89. The second enzyme, encoded by the gene yeiN (EC 4.2.1.70) belonging to the same operon as yeiC, catalyzes the conversion of pseudouridine 5'-phosphate to uracil and ribose 5-phosphate in a divalent cation-dependent manner Escherichia coli ADP + pseudouridine 5'-phosphate
-
?
2.7.1.83 additional information no activity with: uridine, adenosine, guanosine, or cytidine Escherichia coli ?
-
?
4.2.1.70 additional information activity measurement in a two-step assay Thermotoga maritima ?
-
?
4.2.1.70 additional information measuring the production of ribose 5-phosphate with a ribose-5-phosphate isomerase/ribulose-5-phosphate reductase-coupled assay, no activity with ribonucleotide monophosphates AMP, UMP, GMP, and CMP, overview Escherichia coli ?
-
?
4.2.1.70 uracil + D-ribose 5-phosphate
-
Escherichia coli pseudouridine 5'-phosphate + H2O
-
r
4.2.1.70 uracil + D-ribose 5-phosphate the association of IndA with pseudouridine kinase indicates that it serves physiologically to metabolize pseudouridine 5'-phosphate rather than to form it Thermotoga maritima pseudouridine 5'-phosphate + H2O
-
r
4.2.1.70 uracil + D-ribose 5-phosphate the enzyme is involved in the metabolism of pseudouridine in uropathogenic Escherichia coli Escherichia coli pseudouridine 5'-phosphate + H2O
-
r
4.2.1.70 uracil + D-ribose 5-phosphate IndA catalyzes the conversion of pseudouridine 5'-phosphate to uracil and ribose 5-phosphate in a divalent cation-dependent manner by cleavage of the glycosidic C-C bond of pseudouridine Thermotoga maritima pseudouridine 5'-phosphate + H2O
-
r

Synonyms

EC Number Synonyms Comment Organism
2.7.1.83 YeiC
-
Escherichia coli
4.2.1.70 IndA
-
Thermotoga maritima
4.2.1.70 pseudouridine-5'-phosphate glycosidase
-
Thermotoga maritima
4.2.1.70 pseudouridine-5'-phosphate glycosidase
-
Escherichia coli
4.2.1.70 YeiN
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.70 30
-
assay at, both reaction directions Thermotoga maritima
4.2.1.70 30
-
assay at, both reaction directions Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.70 50
-
no activity at or below Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.70 7.1
-
assay at, both reaction directions Thermotoga maritima
4.2.1.70 7.1
-
assay at, both reaction directions Escherichia coli