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Literature summary extracted from

  • Park, J.H.; Burns, K.; Kinsland, C.; Begley, T.P.
    Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase (2004), J. Bacteriol., 186, 1571-1573.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.35 expressed as His-tag fusion protein in Escherichia coli BL21(DE3) Bacillus subtilis
2.7.1.49 gene annotated ThiD, instead of YjbV, subcloning in Escherichia coli strain DH5alpha, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.35 0.047
-
 pyridoxal pH 8, 37°C Bacillus subtilis
2.7.1.35 2.03
-
 4-Amino-5-hydroxymethyl-2-methylpyrimidine pH 8, 37°C Bacillus subtilis
2.7.1.49 additional information
-
 additional information
-
 Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.49 Mg2+ MgCl2 at 2 mM Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.35 ATP + pyridoxal Bacillus subtilis generates the active form of vitamin B6, which serves as cofactor for many enzymes ADP + pyridoxal 5'-phosphate
-
 ?
2.7.1.49 ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine Bacillus subtilis
-
 ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
 ?
2.7.1.49 ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine Bacillus subtilis enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
 ?
2.7.1.49 additional information Bacillus subtilis the enzyme has both a biosynthetic and a salvage pathway function ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.35 Bacillus subtilis
-
-
-
2.7.1.49 Bacillus subtilis
-
 gene annotated ThiD, instead of YjbV
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.35 recombinant protein using His-tag Bacillus subtilis
2.7.1.49 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.35 ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
-
 Bacillus subtilis ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
 ?
2.7.1.35 ATP + pyridoxal
-
 Bacillus subtilis ADP + pyridoxal 5'-phosphate
-
 ?
2.7.1.35 ATP + pyridoxal generates the active form of vitamin B6, which serves as cofactor for many enzymes Bacillus subtilis ADP + pyridoxal 5'-phosphate
-
 ?
2.7.1.35 ATP + pyridoxamine
-
 Bacillus subtilis ADP + pyridoxamine 5'-phosphate
-
 ?
2.7.1.35 ATP + pyridoxine
-
 Bacillus subtilis ADP + pyridoxine 5'-phosphate
-
 ?
2.7.1.49 ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
-
 Bacillus subtilis ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
 ?
2.7.1.49 ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase Bacillus subtilis ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
 ?
2.7.1.49 additional information the enzyme has both a biosynthetic and a salvage pathway function Bacillus subtilis ?
-
 ?
2.7.1.49 additional information no activity with pyridoxal, pyridoxine, or pyridoxamine Bacillus subtilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.35 PdxK formerly ThiD Bacillus subtilis
2.7.1.49 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase
-
 Bacillus subtilis
2.7.1.49 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase
-
 Bacillus subtilis
2.7.1.49 ThiD
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.49 37
-
 assay at Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.35 0.032
-
 pyridoxal pH 8, 37°C Bacillus subtilis
2.7.1.35 0.36
-
 4-Amino-5-hydroxymethyl-2-methylpyrimidine pH 8, 37°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.49 8
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.49 ATP
-
 Bacillus subtilis