Structural Analysis of New Syringopeptins by Tandem Mass Spectrometry

Akira Isogai; Akira Isogai; Haruhisa Iguchi; Jiro Nakayama; Akinori Suzuki; Akihiko Kusai; Jon Y. Takemoto

doi:10.1271/bbb.59.1374

Structural Analysis of New Syringopeptins by Tandem Mass Spectrometry

Akira Isogai, Akira Isogai, Haruhisa Iguchi, Jiro Nakayama, Akinori Suzuki, Akihiko Kusai, Jon Y. Takemoto

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

New syringopeptins SP(SC)-1 and -2 were isolated from culture filtrates of phytopathogenic bacterium strain SC1 of Pseudomonas syringae pv. syringae. These syringopeptins were composed of a β-hydroxy fatty acid, a long sequence of aliphatic amino acids, and a lactone moiety of eight amino acids. The amino acid sequences were deduced from a comparison of their tandem mass sepctra with those of known syringopeptins SP-22a and SP-25a. SP(SC)-1 and SP(SC)-2 resembled SP-22a, but differed from the latter by 3 amino acids.

Original language	English
Pages (from-to)	1374-1376
Number of pages	3
Journal	Bioscience, biotechnology, and biochemistry
Volume	59
Issue number	7
DOIs	https://doi.org/10.1271/bbb.59.1374
Publication status	Published - 1995
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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title = "Structural Analysis of New Syringopeptins by Tandem Mass Spectrometry",

abstract = "New syringopeptins SP(SC)-1 and -2 were isolated from culture filtrates of phytopathogenic bacterium strain SC1 of Pseudomonas syringae pv. syringae. These syringopeptins were composed of a β-hydroxy fatty acid, a long sequence of aliphatic amino acids, and a lactone moiety of eight amino acids. The amino acid sequences were deduced from a comparison of their tandem mass sepctra with those of known syringopeptins SP-22a and SP-25a. SP(SC)-1 and SP(SC)-2 resembled SP-22a, but differed from the latter by 3 amino acids.",

author = "Akira Isogai and Akira Isogai and Haruhisa Iguchi and Jiro Nakayama and Akinori Suzuki and Akihiko Kusai and Takemoto, {Jon Y.}",

year = "1995",

doi = "10.1271/bbb.59.1374",

language = "English",

volume = "59",

pages = "1374--1376",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "7",

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TY - JOUR

T1 - Structural Analysis of New Syringopeptins by Tandem Mass Spectrometry

AU - Isogai, Akira

AU - Iguchi, Haruhisa

AU - Nakayama, Jiro

AU - Suzuki, Akinori

AU - Kusai, Akihiko

AU - Takemoto, Jon Y.

PY - 1995

Y1 - 1995

N2 - New syringopeptins SP(SC)-1 and -2 were isolated from culture filtrates of phytopathogenic bacterium strain SC1 of Pseudomonas syringae pv. syringae. These syringopeptins were composed of a β-hydroxy fatty acid, a long sequence of aliphatic amino acids, and a lactone moiety of eight amino acids. The amino acid sequences were deduced from a comparison of their tandem mass sepctra with those of known syringopeptins SP-22a and SP-25a. SP(SC)-1 and SP(SC)-2 resembled SP-22a, but differed from the latter by 3 amino acids.

AB - New syringopeptins SP(SC)-1 and -2 were isolated from culture filtrates of phytopathogenic bacterium strain SC1 of Pseudomonas syringae pv. syringae. These syringopeptins were composed of a β-hydroxy fatty acid, a long sequence of aliphatic amino acids, and a lactone moiety of eight amino acids. The amino acid sequences were deduced from a comparison of their tandem mass sepctra with those of known syringopeptins SP-22a and SP-25a. SP(SC)-1 and SP(SC)-2 resembled SP-22a, but differed from the latter by 3 amino acids.

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DO - 10.1271/bbb.59.1374

M3 - Article

C2 - 7670202

AN - SCOPUS:0029337446

SN - 0916-8451

VL - 59

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EP - 1376

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 7

ER -

Structural Analysis of New Syringopeptins by Tandem Mass Spectrometry

Abstract

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