Purification and Properties of .GAMMA.-Glutamyltranspeptidase from Bacillus subtilis (natto)
| Autor: | Hiroshi Hosoyama, Yoshihiro Ogawa, Hiroshi Motai, Mitsutoshi Hamano |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Protein subunit
Molecular Sequence Data Bacillus subtilis medicine.disease_cause General Biochemistry Genetics and Molecular Biology Substrate Specificity Enzyme Stability medicine Amino Acid Sequence Incubation Escherichia coli Peptide sequence chemistry.chemical_classification biology Chemistry Temperature gamma-Glutamyltransferase Hydrogen-Ion Concentration biology.organism_classification Acceptor Molecular Weight Glutamine Enzyme Carbohydrate Sequence Polyglutamic Acid Biochemistry General Agricultural and Biological Sciences |
| Zdroj: | Agricultural and Biological Chemistry. 55:2971-2977 |
| ISSN: | 1881-1280 0002-1369 |
| Popis: | To understand the mechanism by which gamma-polyglutamic acid (gamma-PGA) in the sticky material of natto was synthesized, we purified the gamma-glutamyltranspeptidase (gamma-GTP) (EC 2.3.2.2) from the culture broth of Bacillus subtilis (natto) to homogeneity. gamma-GTP was composed of two subunits with molecular weight of 45,000 and 22,000. The N-terminal amino acid sequence of light subunit was homologous with that of gamma-GTP from Escherichia coli. The optimum pH and temperature of activity were 8.5 and 60 degrees C. The enzyme was inactivated by incubation for 15 min at pH 8.0 and 55 degrees C, but little loss of the activity was detected at 40 degrees C. gamma-GTP used glutamine as a gamma-glutamyl donor and acceptor for gamma-PGA synthesis. Dipeptides were better gamma-glutamyl acceptors than free amino acids. |
| Databáze: | OpenAIRE |
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