Novel properties of γ-glutamyltransferase from Pseudomonas syringae with β-aspartyltransferase activity

Asep A. Prihanto; Yuki Nonomura; Kazuyoshi Takagi; Ryosuke Naohara; Midori Umekawa; Mamoru Wakayama

doi:10.1007/s10529-015-1906-1

Novel properties of γ-glutamyltransferase from Pseudomonas syringae with β-aspartyltransferase activity

Asep A. Prihanto
, Yuki Nonomura
, Kazuyoshi Takagi
, Ryosuke Naohara
, Midori Umekawa
, Mamoru Wakayama^*

^*Corresponding author for this work

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

4 Citations (Scopus)

Abstract

Objectives: Gene cloning, purification, and characterization of γ-glutamyltransferase from Pseudomonas syringae (PsGGT) were performed in Escherichia coli. Results: PsGGT was partially purified to 13-fold, with a specific activity of 0.92 U/mg. The molecule is presumed to be a heterodimeric consisting of large (37 kDa) and small (21 kDa) subunits. The optimal pH and temperature for hydrolytic activity were 8 and 37 °C, and those for transfer activity were 9 and 50 °C, respectively. PsGGT could transfer β-aspartyl moiety from asparagine to hydroxylamine and the γ-glutamyl moiety from glutamine to hydroxylamine. Conclusion: PsGGT demonstrated novel functionality on both γ-glutamyltransferase and β-aspartyltransferase.

Original language	English
Pages (from-to)	2255-2263
Number of pages	9
Journal	Biotechnology Letters
Volume	37
Issue number	11
DOIs	https://doi.org/10.1007/s10529-015-1906-1
Publication status	Published - 29 Nov 2015
Externally published	Yes

Keywords

Pseudomonas syringae
β-Aspartyl hydroxamate
β-Aspartyltransferase
γ-Glutamyltransferase

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10.1007/s10529-015-1906-1

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title = "Novel properties of γ-glutamyltransferase from Pseudomonas syringae with β-aspartyltransferase activity",

abstract = "Objectives: Gene cloning, purification, and characterization of γ-glutamyltransferase from Pseudomonas syringae (PsGGT) were performed in Escherichia coli. Results: PsGGT was partially purified to 13-fold, with a specific activity of 0.92 U/mg. The molecule is presumed to be a heterodimeric consisting of large (37 kDa) and small (21 kDa) subunits. The optimal pH and temperature for hydrolytic activity were 8 and 37 °C, and those for transfer activity were 9 and 50 °C, respectively. PsGGT could transfer β-aspartyl moiety from asparagine to hydroxylamine and the γ-glutamyl moiety from glutamine to hydroxylamine. Conclusion: PsGGT demonstrated novel functionality on both γ-glutamyltransferase and β-aspartyltransferase.",

keywords = "Pseudomonas syringae, β-Aspartyl hydroxamate, β-Aspartyltransferase, γ-Glutamyltransferase",

author = "Prihanto, \{Asep A.\} and Yuki Nonomura and Kazuyoshi Takagi and Ryosuke Naohara and Midori Umekawa and Mamoru Wakayama",

note = "Publisher Copyright: {\textcopyright} 2015, Springer Science+Business Media Dordrecht.",

year = "2015",

month = nov,

day = "29",

doi = "10.1007/s10529-015-1906-1",

language = "English",

volume = "37",

pages = "2255--2263",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

number = "11",

}

TY - JOUR

T1 - Novel properties of γ-glutamyltransferase from Pseudomonas syringae with β-aspartyltransferase activity

AU - Prihanto, Asep A.

AU - Nonomura, Yuki

AU - Takagi, Kazuyoshi

AU - Naohara, Ryosuke

AU - Umekawa, Midori

AU - Wakayama, Mamoru

PY - 2015/11/29

Y1 - 2015/11/29

N2 - Objectives: Gene cloning, purification, and characterization of γ-glutamyltransferase from Pseudomonas syringae (PsGGT) were performed in Escherichia coli. Results: PsGGT was partially purified to 13-fold, with a specific activity of 0.92 U/mg. The molecule is presumed to be a heterodimeric consisting of large (37 kDa) and small (21 kDa) subunits. The optimal pH and temperature for hydrolytic activity were 8 and 37 °C, and those for transfer activity were 9 and 50 °C, respectively. PsGGT could transfer β-aspartyl moiety from asparagine to hydroxylamine and the γ-glutamyl moiety from glutamine to hydroxylamine. Conclusion: PsGGT demonstrated novel functionality on both γ-glutamyltransferase and β-aspartyltransferase.

AB - Objectives: Gene cloning, purification, and characterization of γ-glutamyltransferase from Pseudomonas syringae (PsGGT) were performed in Escherichia coli. Results: PsGGT was partially purified to 13-fold, with a specific activity of 0.92 U/mg. The molecule is presumed to be a heterodimeric consisting of large (37 kDa) and small (21 kDa) subunits. The optimal pH and temperature for hydrolytic activity were 8 and 37 °C, and those for transfer activity were 9 and 50 °C, respectively. PsGGT could transfer β-aspartyl moiety from asparagine to hydroxylamine and the γ-glutamyl moiety from glutamine to hydroxylamine. Conclusion: PsGGT demonstrated novel functionality on both γ-glutamyltransferase and β-aspartyltransferase.

KW - Pseudomonas syringae

KW - β-Aspartyl hydroxamate

KW - β-Aspartyltransferase

KW - γ-Glutamyltransferase

UR - https://www.scopus.com/pages/publications/84942500258

U2 - 10.1007/s10529-015-1906-1

DO - 10.1007/s10529-015-1906-1

M3 - Article

C2 - 26149579

AN - SCOPUS:84942500258

SN - 0141-5492

VL - 37

SP - 2255

EP - 2263

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 11

ER -

Novel properties of γ-glutamyltransferase from Pseudomonas syringae with β-aspartyltransferase activity

Abstract

Keywords

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