Asymmetric decarboxylation of α-hydroxy- and α-amino-α-phenylmalonate catalyzed by arylmalonate decarboxylase from Alcaligenes bronchisepticus

Keisuke Tamura, Yosuke Terao, Kenji Miyamoto, Hiromichi Ohta

研究成果: Article

9 引用 (Scopus)

抄録

Arylmalonate decarboxylase (EC 4.1.1.76, from Alcaligenes bronchisepticus KU 1201) is an enzyme that catalyzes asymmetric decarboxylation of arylmalonate. The enzyme accepts as substrates compounds that have a sterically small hydrophobic α-substituent, such as H, F, and methyl. To widen the applicability of this enzyme and to obtain information on the interaction between the enzyme and substrates, we tried the reaction of compounds with a hydrophilic substituent. Although the relative reactivities were lower compared to that of phenylmalonate, α-hydroxy- and α-aminophenylmalonate were decarboxylated to give optically active monobasic acids.

元の言語English
ページ(範囲)253-257
ページ数5
ジャーナルBiocatalysis and Biotransformation
26
発行部数4
DOI
出版物ステータスPublished - 2008 7

Fingerprint

Alcaligenes
Decarboxylation
Enzymes
Substrates
Acids
malonate decarboxylase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Catalysis

これを引用

@article{b81f2e5e07e24fe4b0f62c4060276bf2,
title = "Asymmetric decarboxylation of α-hydroxy- and α-amino-α-phenylmalonate catalyzed by arylmalonate decarboxylase from Alcaligenes bronchisepticus",
abstract = "Arylmalonate decarboxylase (EC 4.1.1.76, from Alcaligenes bronchisepticus KU 1201) is an enzyme that catalyzes asymmetric decarboxylation of arylmalonate. The enzyme accepts as substrates compounds that have a sterically small hydrophobic α-substituent, such as H, F, and methyl. To widen the applicability of this enzyme and to obtain information on the interaction between the enzyme and substrates, we tried the reaction of compounds with a hydrophilic substituent. Although the relative reactivities were lower compared to that of phenylmalonate, α-hydroxy- and α-aminophenylmalonate were decarboxylated to give optically active monobasic acids.",
keywords = "α-aminomalonate, α-hydroxymalonate, Arylmalonate decarboxylase, Enzymatic decarboxylation",
author = "Keisuke Tamura and Yosuke Terao and Kenji Miyamoto and Hiromichi Ohta",
year = "2008",
month = "7",
doi = "10.1080/10242420701685668",
language = "English",
volume = "26",
pages = "253--257",
journal = "Biocatalysis and Biotransformation",
issn = "1024-2422",
publisher = "Informa Healthcare",
number = "4",

}

TY - JOUR

T1 - Asymmetric decarboxylation of α-hydroxy- and α-amino-α-phenylmalonate catalyzed by arylmalonate decarboxylase from Alcaligenes bronchisepticus

AU - Tamura, Keisuke

AU - Terao, Yosuke

AU - Miyamoto, Kenji

AU - Ohta, Hiromichi

PY - 2008/7

Y1 - 2008/7

N2 - Arylmalonate decarboxylase (EC 4.1.1.76, from Alcaligenes bronchisepticus KU 1201) is an enzyme that catalyzes asymmetric decarboxylation of arylmalonate. The enzyme accepts as substrates compounds that have a sterically small hydrophobic α-substituent, such as H, F, and methyl. To widen the applicability of this enzyme and to obtain information on the interaction between the enzyme and substrates, we tried the reaction of compounds with a hydrophilic substituent. Although the relative reactivities were lower compared to that of phenylmalonate, α-hydroxy- and α-aminophenylmalonate were decarboxylated to give optically active monobasic acids.

AB - Arylmalonate decarboxylase (EC 4.1.1.76, from Alcaligenes bronchisepticus KU 1201) is an enzyme that catalyzes asymmetric decarboxylation of arylmalonate. The enzyme accepts as substrates compounds that have a sterically small hydrophobic α-substituent, such as H, F, and methyl. To widen the applicability of this enzyme and to obtain information on the interaction between the enzyme and substrates, we tried the reaction of compounds with a hydrophilic substituent. Although the relative reactivities were lower compared to that of phenylmalonate, α-hydroxy- and α-aminophenylmalonate were decarboxylated to give optically active monobasic acids.

KW - α-aminomalonate

KW - α-hydroxymalonate

KW - Arylmalonate decarboxylase

KW - Enzymatic decarboxylation

UR - http://www.scopus.com/inward/record.url?scp=45849148026&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=45849148026&partnerID=8YFLogxK

U2 - 10.1080/10242420701685668

DO - 10.1080/10242420701685668

M3 - Article

AN - SCOPUS:45849148026

VL - 26

SP - 253

EP - 257

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

SN - 1024-2422

IS - 4

ER -