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Literature summary for 3.4.19.9 extracted from

  • Tanaka, T.; Hiruta, O.; Futamura, T.; Uotani, K.; Satoh, A.; Taniguchi, M.; Or, S.
    Purification and characterization of poly(g-glutamic acid) hydrolase from a filamentous fungus, Myrothecium sp. TM-4222 (1993), Biosci. Biotechnol. Biochem., 57, 2148-2153.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ weak Myrothecium sp.
EDTA no inhibition Myrothecium sp.
additional information no inhibition by competitive inhibitors of serine and cysteine proteinases; no inhibition by phosphoramidon Myrothecium sp.
PCMB
-
Myrothecium sp.
Phenylmethylsulfonylfluoride no inhibition Myrothecium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
68000
-
gel filtration Myrothecium sp.

Organism

Organism UniProt Comment Textmining
Myrothecium sp.
-
TM-4222
-
Myrothecium sp. TM-4222
-
TM-4222
-

Purification (Commentary)

Purification (Comment) Organism
-
Myrothecium sp.

Source Tissue

Source Tissue Comment Organism Textmining
culture filtrate
-
Myrothecium sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Myrothecium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly-Glu + H2O enzyme is specific for poly(gamma-glutamic) acid, but not for other gamma-glutamyl peptides or amides Myrothecium sp. ? endo-type specificity, 38% of the original poly-Glu with an average MW of 500000 is converted to smaller peptides, and then depolymerized to a mixture of gamma-oligopeptides which consist of only L-glutamic acid, L-glutamic acid monomer is negligible in the reaction mixture, the remaining 62% of poly(gamma-glutamic acid) are resistant to the enzyme action ?
poly-Glu + H2O enzyme is specific for poly(gamma-glutamic) acid, but not for other gamma-glutamyl peptides or amides Myrothecium sp. TM-4222 ? endo-type specificity, 38% of the original poly-Glu with an average MW of 500000 is converted to smaller peptides, and then depolymerized to a mixture of gamma-oligopeptides which consist of only L-glutamic acid, L-glutamic acid monomer is negligible in the reaction mixture, the remaining 62% of poly(gamma-glutamic acid) are resistant to the enzyme action ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Myrothecium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
stable up to, 1 h, pH 5.0 Myrothecium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Myrothecium sp.
7.8
-
-
Myrothecium sp.