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Literature summary for 6.1.1.15 extracted from

  • Norris, R.D.; Fowden, L.
    Cold-lability of prolyl-tRNA synthetase from higher plants (1974), Phytochemistry, 13, 1677-1687.
No PubMed abstract available
Search for more literature for 6.1.1.15

General Stability

General Stability Organism
ATP, Pro and several Pro analogues prevent inactivation at 0°C Phaseolus vulgaris
ATP, Pro and several Pro analogues prevent inactivation at 0°C Delonix regia
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C Phaseolus vulgaris
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C Delonix regia
rapid and reversible photoinactivation in absence of methylene blue. ATP or Pro protects Delonix regia
the time taken for 4 M urea to reduced the activity by 50% is increased in presence of 15% glycerol from 0.7 min to 7 min and from 0.3 min to 1.5 min for the Phaseolus and Delonix enzymes respectively Phaseolus vulgaris
the time taken for 4 M urea to reduced the activity by 50% is increased in presence of 15% glycerol from 0.7 min to 7 min and from 0.3 min to 1.5 min for the Phaseolus and Delonix enzymes respectively Delonix regia

Inhibitors

Inhibitors Comment Organism Structure
p-chloromercuribenzoate ATP, tRNA, Pro or several analogues of Pro, protect against inhibition. Reactivation by sulfhydryl-reducing reagents, reactivation of Delonix enzyme is markedly temperature-dependent, Phaseolus enzyme is reactivated equally efficiently at all temperatures tested Delonix regia
p-chloromercuribenzoate ATP, tRNA, Pro or several analogues of Pro, protect against inhibition. Reactivation by sulfhydryl-reducing reagents, reactivation of Delonix enzyme is markedly temperature-dependent, Phaseolus enzyme is reactivated equally efficiently at all temperatures tested Phaseolus vulgaris

Organism

Organism UniProt Comment Textmining
Delonix regia
-
-
-
Phaseolus vulgaris
-
-
-

Storage Stability

Storage Stability Organism
0.1 M Tris-maleate KOH buffer, pH 7.0, about 80% loss of activity in ATP-diphosphate exchange Delonix regia
0.1 M Tris-maleate KOH buffer, pH 8.0, about 85% loss of activity in ATP-diphosphate exchange Delonix regia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-proline + tRNAPro
-
 Phaseolus vulgaris AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro
-
 Delonix regia AMP + diphosphate + L-prolyl-tRNAPro
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the enzyme from a number of higher plants that producing azetidine -2-carboxylic acid (A2C) is more rapidly inactivated in the cold than the enzyme from plants which do not contain A2C Phaseolus vulgaris
additional information
-
 the enzyme from a number of higher plants that producing azetidine -2-carboxylic acid (A2C) is more rapidly inactivated in the cold than the enzyme from plants which do not contain A2C Delonix regia
additional information
-
 ATP, Pro and several Pro analogues prevent inactivation at 0°C Phaseolus vulgaris
additional information
-
 ATP, Pro and several Pro analogues prevent inactivation at 0°C Delonix regia
additional information
-
 inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C Phaseolus vulgaris
additional information
-
 inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C Delonix regia
2
-
 complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol Phaseolus vulgaris
2
-
 complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol Delonix regia