Activities and properties of putrescine-biosynthetic enzymes in Vibrio parahaemolyticus

S. Yamamoto, H. Nakao, K. Yamasaki, K. Takashina, Y. Suemoto, S. Shinoda

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The biosynthetic pathways for putrescine (Put) in Vibrio parahaemolyticus were delineated by measuring activities of the enzymes which would be involved in its biosynthesis. Experiments with labeled arginine and ornithine revealed that both of these amino acids were converted into Put by intact cells. The activities of three enzymes, arginine decarboxylase (ADC), ornithine decarboxylase (ODC), and agmatine ureohydrolase (AUH), were detected in cell extracts. ADC and ODC of V. parahaemolyticus were similar in the following properties to the corresponding enzymes of Escherichia coli: 1) both decarboxylases showed a pH optimum at 8.25 and required pyridoxal phosphate and dithiothreitol for full activity; 2) while ODC was considerably activated by GTP, ADC was only slightly; 3) both decarboxylases were inhibited by polyamines; 4) ADC was inhibited by difluoromethylarginine, a potent inhibitor of bacterial ADC. However, in contrast to the corresponding enzymes of E. coli, the V. parahaemolyticus ADC showed no requirement for Mg2+, and the AUH was active over a wide pH range of 8.5-9.5 with a maximum at pH 9.0. Furthermore, in all 6 strains tested, the activity of ADC was obviously high compared with that of ODC, and AUH was present with a relatively high activity. Cultivation of these strains at a suboptimal NaCl concentration (0.5%) resulted in a pronounced increase in both ADC and AUH activities. These observations suggest that the important pathway for Put biosynthesis in V. parahaemolyticus is the decarboxylation of arginine by ADC and the subsequent hydrolysis of its product, agmatine, by AUH.

Original languageEnglish
Pages (from-to)675-687
Number of pages13
JournalMicrobiology and Immunology
Volume32
Issue number7
Publication statusPublished - 1988

Fingerprint

Vibrio parahaemolyticus
Putrescine
Ornithine Decarboxylase
Enzymes
Carboxy-Lyases
Arginine
Agmatine
Escherichia coli
arginine decarboxylase
Decarboxylation
Pyridoxal Phosphate
Ornithine
Dithiothreitol
Biosynthetic Pathways
Polyamines
Guanosine Triphosphate
Cell Extracts
Hydrolysis
agmatinase
Amino Acids

ASJC Scopus subject areas

  • Immunology and Microbiology(all)
  • Microbiology
  • Microbiology (medical)

Cite this

Yamamoto, S., Nakao, H., Yamasaki, K., Takashina, K., Suemoto, Y., & Shinoda, S. (1988). Activities and properties of putrescine-biosynthetic enzymes in Vibrio parahaemolyticus. Microbiology and Immunology, 32(7), 675-687.

Activities and properties of putrescine-biosynthetic enzymes in Vibrio parahaemolyticus. / Yamamoto, S.; Nakao, H.; Yamasaki, K.; Takashina, K.; Suemoto, Y.; Shinoda, S.

In: Microbiology and Immunology, Vol. 32, No. 7, 1988, p. 675-687.

Research output: Contribution to journalArticle

Yamamoto, S, Nakao, H, Yamasaki, K, Takashina, K, Suemoto, Y & Shinoda, S 1988, 'Activities and properties of putrescine-biosynthetic enzymes in Vibrio parahaemolyticus', Microbiology and Immunology, vol. 32, no. 7, pp. 675-687.
Yamamoto S, Nakao H, Yamasaki K, Takashina K, Suemoto Y, Shinoda S. Activities and properties of putrescine-biosynthetic enzymes in Vibrio parahaemolyticus. Microbiology and Immunology. 1988;32(7):675-687.
Yamamoto, S. ; Nakao, H. ; Yamasaki, K. ; Takashina, K. ; Suemoto, Y. ; Shinoda, S. / Activities and properties of putrescine-biosynthetic enzymes in Vibrio parahaemolyticus. In: Microbiology and Immunology. 1988 ; Vol. 32, No. 7. pp. 675-687.
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