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Literature summary extracted from

  • Narayanan, S.S.; Ramanujan, A.; Krishna, S.; Nampoothiri, K.M.
    Purification and biochemical characterization of methionine aminopeptidase (MetAP) from Mycobacterium smegmatis mc2155 (2008), Appl. Biochem. Biotechnol., 151, 512-521.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.18 2-mercaptoethanol complete inhibition at 10 mM Mycolicibacterium smegmatis
3.4.11.18 actinonin 12.6% relative activity at 0.05 mM Mycolicibacterium smegmatis
3.4.11.18 amastatin 29.7% relative activity at 0.05 mM Mycolicibacterium smegmatis
3.4.11.18 bestatin 44.9% relative activity at 0.05 mM Mycolicibacterium smegmatis
3.4.11.18 Cu2+
-
 Mycolicibacterium smegmatis
3.4.11.18 EDTA 33.7% relative activity at 100 mM, the enzyme activity inhibited by 1 mM EDTA is restored in presence of 5 mM Mg2+ Mycolicibacterium smegmatis
3.4.11.18 Fe2+
-
 Mycolicibacterium smegmatis
3.4.11.18 K+
-
 Mycolicibacterium smegmatis
3.4.11.18 phenylmethylsulfonyl fluoride 29.4% relative activity at 5 mM Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.18 Co2+ the enzyme activity is enhanced by 1 mM Co2+ Mycolicibacterium smegmatis
3.4.11.18 Mg2+ the enzyme activity is enhanced 2fold by 1 mM Mg2+ Mycolicibacterium smegmatis
3.4.11.18 Na+ some positive effect on the enzyme activity at 5 mM Mycolicibacterium smegmatis
3.4.11.18 NH4+ some positive effect on the enzyme activity at 5 mM Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.18 32000
-
 the calculated molecular weight from nucleotide-derived amino acid sequence is about 32000 Da Mycolicibacterium smegmatis
3.4.11.18 37000
-
 SDS-PAGE Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.18 Mycolicibacterium smegmatis
-
-
-
3.4.11.18 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.18 ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephadex G-100 gel filtration Mycolicibacterium smegmatis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.11.18 0.74
-
 crude extract, at 50°C Mycolicibacterium smegmatis
3.4.11.18 16.2
-
 after 22fold purification, at 50°C Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.18 L-Met-p-nitroanilide + H2O
-
 Mycolicibacterium smegmatis L-Met + p-nitroaniline
-
 ?
3.4.11.18 L-Met-p-nitroanilide + H2O
-
 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 L-Met + p-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.18 MetAP
-
 Mycolicibacterium smegmatis
3.4.11.18 methionine aminopeptidase
-
 Mycolicibacterium smegmatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.18 50
-
 optimum temperature for MetAP activity against the substrate L-Met p-nitroanilide Mycolicibacterium smegmatis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.18 50 65 the enzyme is stable at 50 °C with half-life of more than 8 h, at 50°C and 55°C, the enzyme shows stable activity over a period of 1 h with only a slight decrease of 10% in activity, at 60 °C the relative activity decreases to 50% within 50 min, whereas at 65°C the relative activity decreases to 19% and declines to 0 after a period of 50 min Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.18 8.5
-
-
 Mycolicibacterium smegmatis