Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica

Ildar I. Mustakhimov; Olga N. Rozova; Alexander S. Reshetnikov; Valentina N. Khmelenina; J. Colin Murrell; Yuri A. Trotsenko

doi:10.1111/j.1574-6968.2008.01156.x

Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica

Ildar I. Mustakhimov, Olga N. Rozova, Alexander S. Reshetnikov, Valentina N. Khmelenina, J. Colin Murrell, Yuri A. Trotsenko

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

11 Citations (Scopus)

Abstract

Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to ?-N-acetyl-a,?-diaminobutyrate with acetyl coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 °C), Km for diaminobutyrate (370 or 375 µM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions.

Original language	English
Pages (from-to)	91-96
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	283
Issue number	1
DOIs	https://doi.org/10.1111/j.1574-6968.2008.01156.x
Publication status	Published - 2008

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10.1111/j.1574-6968.2008.01156.x

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@article{0c06e935802d4fe8a63252d5e76582d3,

title = "Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica",

abstract = "Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to ?-N-acetyl-a,?-diaminobutyrate with acetyl coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 °C), Km for diaminobutyrate (370 or 375 µM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions.",

author = "Mustakhimov, {Ildar I.} and Rozova, {Olga N.} and Reshetnikov, {Alexander S.} and Khmelenina, {Valentina N.} and Murrell, {J. Colin} and Trotsenko, {Yuri A.}",

year = "2008",

doi = "10.1111/j.1574-6968.2008.01156.x",

language = "English",

volume = "283",

pages = "91--96",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Wiley",

number = "1",

}

Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica. / Mustakhimov, Ildar I.; Rozova, Olga N.; Reshetnikov, Alexander S.; Khmelenina, Valentina N.; Murrell, J. Colin; Trotsenko, Yuri A.

In: FEMS Microbiology Letters, Vol. 283, No. 1, 2008, p. 91-96.

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

TY - JOUR

T1 - Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica

AU - Mustakhimov, Ildar I.

AU - Rozova, Olga N.

AU - Reshetnikov, Alexander S.

AU - Khmelenina, Valentina N.

AU - Murrell, J. Colin

AU - Trotsenko, Yuri A.

PY - 2008

Y1 - 2008

N2 - Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to ?-N-acetyl-a,?-diaminobutyrate with acetyl coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 °C), Km for diaminobutyrate (370 or 375 µM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions.

AB - Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to ?-N-acetyl-a,?-diaminobutyrate with acetyl coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 °C), Km for diaminobutyrate (370 or 375 µM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions.

U2 - 10.1111/j.1574-6968.2008.01156.x

DO - 10.1111/j.1574-6968.2008.01156.x

M3 - Article

VL - 283

SP - 91

EP - 96

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

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