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Literature summary extracted from

  • Ruhlmann, A.; Cramer, F.; Englisch, U.
    Isolation and analysis of mutated histidyl-tRNA synthetases from Escherichia coli (1997), Biochem. Biophys. Res. Commun., 237, 192-201.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.21 V-HisRS-R259K mutants: V-HisRS-R259K, V-HisRS-R259Q, des(A2-G10)-HisRS, des(A2-Q6)-HisRS, V-His-RS with N-terminal addition of valine, and M-HisRS with N-terminal addition of methionine. N-terminal addition of either methionine or valine, or the deletion of 6 amino terminal amino acids deceases the specific aminoacylation activity 2fold to 7fold. Further N-terminal deletions of 10 or 17 amino acids causes 100fold reduced aminoacylation and 10fold reduced ATP-diphosphate exchange. Removal of 18 or more amino acids from the N-terminus results in an inactive enzyme mutants. The two point mutations R259Q and R259K, show blocked histidyl-tRNA synthetase activity without affecting histidine or ATP binding Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.21 0.008
-
 His HisRS, aminoacylation Escherichia coli
6.1.1.21 0.011
-
 His mutant enzyme form M-HisRS, aminoacylation Escherichia coli
6.1.1.21 0.017
-
 His mutant enzyme form V-HisRS, mutant enzyme form V-His-RS-R259K, aminoacylation Escherichia coli
6.1.1.21 0.02
-
 His mutant enzyme form des(A2-Q6)-HisRS, aminoacylation Escherichia coli
6.1.1.21 0.06
-
 His mutant enzyme form des(A2-G10)-HisRS, aminoacylation Escherichia coli
6.1.1.21 0.22
-
 ATP mutant enzyme form des(A2-Q6), ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.3
-
 ATP mutant enzyme form V-HisRS-R259K, ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.33
-
 ATP mutant enzyme form V-HisRS-R259Q, ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.35
-
 ATP mutant enzyme form V-HisRS, ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.39
-
 ATP mutant enzyme form M-HisRS, ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.56
-
 ATP HisRS, ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.655
-
 ATP mutant enzyme form des(A2-G10)HisRS, ATP-diphosphate exchange Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.21 Escherichia coli
-
 wild-type and mutants, V-HisRS-R259K, V-HisRS-R259Q, des(A2-G10)-HisRS, des(A2-Q6)-HisRS, V-His-RS (N-terminal addition of valine), and M-HisRS (N-terminal addition of methionine)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.21
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.21 ATP + L-histidine + tRNAHis
-
 Escherichia coli AMP + diphosphate + L-histidyl-tRNAHis
-
 ?
6.1.1.21 additional information ATP-diphosphate exchange Escherichia coli ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.21 0.1
-
 His mutant enzyme form V-HisRS-R259K, aminoacylation Escherichia coli
6.1.1.21 0.2
-
 ATP mutant enzyme form des(A2-G10)-HisRS, ATP-diphosphate exchange Escherichia coli
6.1.1.21 0.4
-
 ATP mutant enzyme form V-HisRS-R259Q, ATP-diphosphate exchange Escherichia coli
6.1.1.21 1
-
 His mutant enzyme form des(A2-G10)-HisRS, aminoacylation Escherichia coli
6.1.1.21 6
-
 His enzyme form with N-terminal addition of methionine M-HisRS, enzyme form with N-terminal addition of valineV-HisRS, aminoacylation Escherichia coli
6.1.1.21 7
-
 His wild-type HisRS, aminoacylation Escherichia coli
6.1.1.21 8
-
 ATP enzyme form with N-terminal addition of valine V-HisRS, mutant enzyme form des(A2-Q6)-HisRS, ATP-diphosphate exchange Escherichia coli
6.1.1.21 9
-
 His mutant enzyme form des(A2-Q6)-HisRS, aminoacylation, ATP, and mutant enzyme form with N-terminal addition of methionine M-HisRS, ATP-diphosphate exchange Escherichia coli
6.1.1.21 34
-
 ATP HisRS, ATP-diphosphate exchange Escherichia coli