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Literature summary for 3.1.1.5 extracted from

  • Prabhakaran, K.; Harris, E.B.; Randhawa, B.
    Properties of lysophospholipase in Mycobacterium leprae (1996), J. Basic Microbiol., 36, 341-349.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
AACOCF3 a trifluoromethyl ketone analog of arachidonic acid, uncompetitive Mycobacterium leprae
tricyclodecan-9-yl-xanthogenate potassium
-
Mycobacterium leprae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm two-third of the enzyme is particulate, one-third is cytoplasmic Mycobacterium leprae 5737
-
particle-bound two-third of the enzyme is particulate, one-third is cytoplasmic Mycobacterium leprae
-
-

Organism

Organism UniProt Comment Textmining
Mycobacterium leprae
-
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Mycobacterium leprae

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 50 25°C: about 70% of maximal activity, 50°C: about 90% of maximal activity Mycobacterium leprae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
complete inactivation above Mycobacterium leprae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Mycobacterium leprae

pH Range

pH Minimum pH Maximum Comment Organism
4 7 pH 4.0: about 55% of maximal activity, pH 7.0: about 60% of maximal activity Mycobacterium leprae