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Literature summary 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

General Stability

EC Number General Stability Organism
6.1.1.15 ATP, Pro and several Pro analogues prevent inactivation at 0°C Phaseolus vulgaris
6.1.1.15 ATP, Pro and several Pro analogues prevent inactivation at 0°C Delonix regia
6.1.1.15 inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C Phaseolus vulgaris
6.1.1.15 inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2°C Delonix regia
6.1.1.15 rapid and reversible photoinactivation in absence of methylene blue. ATP or Pro protects Delonix regia
6.1.1.15 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
6.1.1.15 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

EC Number Inhibitors Comment Organism Structure
6.1.1.15 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
6.1.1.15 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

EC Number Organism UniProt Comment Textmining
6.1.1.15 Delonix regia
-
-
-
6.1.1.15 Phaseolus vulgaris
-
-
-

Storage Stability

EC Number Storage Stability Organism
6.1.1.15 0.1 M Tris-maleate KOH buffer, pH 7.0, about 80% loss of activity in ATP-diphosphate exchange Delonix regia
6.1.1.15 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)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.1.1.15 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
6.1.1.15 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
6.1.1.15 additional information
-
 ATP, Pro and several Pro analogues prevent inactivation at 0°C Phaseolus vulgaris
6.1.1.15 additional information
-
 ATP, Pro and several Pro analogues prevent inactivation at 0°C Delonix regia
6.1.1.15 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
6.1.1.15 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
6.1.1.15 2
-
 complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol Phaseolus vulgaris
6.1.1.15 2
-
 complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol Delonix regia