Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast

Takahiro Oba, Shuji Nomiyama, Hideki Hirakawa, Kosuke Tashiro, Satoru Kuhara

研究成果: ジャーナルへの寄稿記事

22 引用 (Scopus)

抄録

We identified a new mutation, Asp578Tyr, in α-isopropylmalate synthase (a LEU4 gene product) that releases leucine feedback inhibition and causes hyperproduction of isoamyl alcohol (i-AmOH) in sake yeast. Spontaneous sake yeast mutants that express resistance to 5,5,5-trifluoro-DL-leucine (TFL) were isolated, and a mutant strain, TFL20, was characterized at the genetic and biochemical levels. An enzyme assay for α-isopropylmalate synthase showed that strain TFL20 was released from feedback inhibition by L-leucine. Furthermore, DNA sequencing of the LEU4 gene for a haploid of the mutant TFL20 revealed that aspartic acid in position 578 changes to tyrosine. A comparison of the three-dimensional structures of wild-type LEU4p and mutant LEU4D578Yp by the homology modeling method showed that Asp578 is important for leucine feedback inhibition. We conclude that the mutation from Asp to Tyr in 578 is a novel change causing release from leucine feedback inhibition.

元の言語英語
ページ(範囲)1270-1273
ページ数4
ジャーナルBioscience, Biotechnology and Biochemistry
69
発行部数7
DOI
出版物ステータス出版済み - 9 1 2005

Fingerprint

Leucine
Yeast
Yeasts
Feedback
Genes
Mutation
Haploidy
Enzyme Assays
DNA Sequence Analysis
Aspartic Acid
Tyrosine
Molecular Biology
Assays
DNA
Enzymes

All Science Journal Classification (ASJC) codes

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

これを引用

Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast. / Oba, Takahiro; Nomiyama, Shuji; Hirakawa, Hideki; Tashiro, Kosuke; Kuhara, Satoru.

:: Bioscience, Biotechnology and Biochemistry, 巻 69, 番号 7, 01.09.2005, p. 1270-1273.

研究成果: ジャーナルへの寄稿記事

Oba, Takahiro ; Nomiyama, Shuji ; Hirakawa, Hideki ; Tashiro, Kosuke ; Kuhara, Satoru. / Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast. :: Bioscience, Biotechnology and Biochemistry. 2005 ; 巻 69, 番号 7. pp. 1270-1273.
@article{d44fd7ece02c4881a12f835f20eadf8b,
title = "Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast",
abstract = "We identified a new mutation, Asp578Tyr, in α-isopropylmalate synthase (a LEU4 gene product) that releases leucine feedback inhibition and causes hyperproduction of isoamyl alcohol (i-AmOH) in sake yeast. Spontaneous sake yeast mutants that express resistance to 5,5,5-trifluoro-DL-leucine (TFL) were isolated, and a mutant strain, TFL20, was characterized at the genetic and biochemical levels. An enzyme assay for α-isopropylmalate synthase showed that strain TFL20 was released from feedback inhibition by L-leucine. Furthermore, DNA sequencing of the LEU4 gene for a haploid of the mutant TFL20 revealed that aspartic acid in position 578 changes to tyrosine. A comparison of the three-dimensional structures of wild-type LEU4p and mutant LEU4D578Yp by the homology modeling method showed that Asp578 is important for leucine feedback inhibition. We conclude that the mutation from Asp to Tyr in 578 is a novel change causing release from leucine feedback inhibition.",
author = "Takahiro Oba and Shuji Nomiyama and Hideki Hirakawa and Kosuke Tashiro and Satoru Kuhara",
year = "2005",
month = "9",
day = "1",
doi = "10.1271/bbb.69.1270",
language = "English",
volume = "69",
pages = "1270--1273",
journal = "Bioscience, Biotechnology and Biochemistry",
issn = "0916-8451",
publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
number = "7",

}

TY - JOUR

T1 - Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast

AU - Oba, Takahiro

AU - Nomiyama, Shuji

AU - Hirakawa, Hideki

AU - Tashiro, Kosuke

AU - Kuhara, Satoru

PY - 2005/9/1

Y1 - 2005/9/1

N2 - We identified a new mutation, Asp578Tyr, in α-isopropylmalate synthase (a LEU4 gene product) that releases leucine feedback inhibition and causes hyperproduction of isoamyl alcohol (i-AmOH) in sake yeast. Spontaneous sake yeast mutants that express resistance to 5,5,5-trifluoro-DL-leucine (TFL) were isolated, and a mutant strain, TFL20, was characterized at the genetic and biochemical levels. An enzyme assay for α-isopropylmalate synthase showed that strain TFL20 was released from feedback inhibition by L-leucine. Furthermore, DNA sequencing of the LEU4 gene for a haploid of the mutant TFL20 revealed that aspartic acid in position 578 changes to tyrosine. A comparison of the three-dimensional structures of wild-type LEU4p and mutant LEU4D578Yp by the homology modeling method showed that Asp578 is important for leucine feedback inhibition. We conclude that the mutation from Asp to Tyr in 578 is a novel change causing release from leucine feedback inhibition.

AB - We identified a new mutation, Asp578Tyr, in α-isopropylmalate synthase (a LEU4 gene product) that releases leucine feedback inhibition and causes hyperproduction of isoamyl alcohol (i-AmOH) in sake yeast. Spontaneous sake yeast mutants that express resistance to 5,5,5-trifluoro-DL-leucine (TFL) were isolated, and a mutant strain, TFL20, was characterized at the genetic and biochemical levels. An enzyme assay for α-isopropylmalate synthase showed that strain TFL20 was released from feedback inhibition by L-leucine. Furthermore, DNA sequencing of the LEU4 gene for a haploid of the mutant TFL20 revealed that aspartic acid in position 578 changes to tyrosine. A comparison of the three-dimensional structures of wild-type LEU4p and mutant LEU4D578Yp by the homology modeling method showed that Asp578 is important for leucine feedback inhibition. We conclude that the mutation from Asp to Tyr in 578 is a novel change causing release from leucine feedback inhibition.

UR - http://www.scopus.com/inward/record.url?scp=23944473673&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=23944473673&partnerID=8YFLogxK

U2 - 10.1271/bbb.69.1270

DO - 10.1271/bbb.69.1270

M3 - Article

C2 - 16041129

AN - SCOPUS:23944473673

VL - 69

SP - 1270

EP - 1273

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 7

ER -