Aliphatic amidase from Rhodococcus rhodochrous M8 is related to the nitrilase/cyanide hydratase family

被引：16

作者：

Pertsovich, SI

Guranda, DT

Podchernyaev, DA

Yanenko, AS

Svedas, VK ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Belozersky Inst Physicochem Biol, Fac Bioengn & Bioinformat, Moscow 119992, Russia

[2] Inst Genet & Select Ind Microorganisms, Moscow 113545, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2005年 / 70卷 / 11期

关键词：

Rhodococcus rhodochrous amidase; sequence alignment; amidase classification; substrate specificity; acrylamide hydrolysis;

D O I：

10.1007/s10541-005-0260-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A comparative study of amino acid sequence and physicochemical properties indicates the affiliation of an amidase from Rhodococcus rhodochrous M8 (EC 3.5.1.4) to the nitrilase/cyanide hydratase family. Cluster analysis and multiple alignments show that Cys166 is an active site nucleophile. The enzyme has been shown to be a typical aliphatic amidase, being the most active toward short-chain linear amides. Small polar molecules such as hydroxylamine and O-methyl hydroxylamine can serve as effective external nucleophiles in acyl transfer reactions. The kinetics of the industrially important amidase-catalyzed acrylamide hydrolysis has been studied over a wide range Of Substrate concentrations; inhibition during enzymatic hydrolysis by the substrate and product (acrylic acid) has been observed, an adequate kinetic scheme has been evaluated and the corresponding kinetic parameters have been determined.

引用

页码：1280 / 1287

页数：8

共 16 条

[1] Aliphatic Amidase from Rhodococcus rhodochrous M8 Is Related to the Nitrilase/Cyanide Hydratase Family
S. I. Pertsovich
D. T. Guranda
D. A. Podchernyaev
A. S. Yanenko
V. K. Svedas
Biochemistry (Moscow), 2005, 70 : 1280 - 1287
[2] Purification and characterization of nitrile hydratase from Rhodococcus rhodochrous M8
Sinolitsky, MK
Rogacheva, SM
Poltavskaya, SV
Sintin, AA
Voronin, SP
ENVIRONMENTAL BIOTECHNOLOGY: PRINCIPLES AND APPLICATIONS, 1996, : 96 - 104
[3] Cloning the amidase gene from Rhodococcus rhodochrous M8 and its expression in Escherichia coli
L. E. Ryabchenko
D. A. Podchernyaev
E. K. Kotlova
A. S. Yanenko
Russian Journal of Genetics, 2006, 42 : 886 - 892
[4] Cloning the amidase gene from Rhodococcus rhodochrous M8 and its expression in Escherichia coli
Ryabchenko, L. E.
Podchernyaev, D. A.
Kotlova, E. K.
Yanenko, A. S.
RUSSIAN JOURNAL OF GENETICS, 2006, 42 (08) : 886 - 892
[5] Cobalt-dependent transcription of the nitrile hydratase gene in Rhodococcus rhodochrous M8
Pogorelova, TE
Ryabchenko, LE
Sunzov, NI
Yanenko, AS
FEMS MICROBIOLOGY LETTERS, 1996, 144 (2-3) : 191 - 195
[6] Structure of the Regulatory Region of Nitrile Hydratase Genes in Rhodococcus rhodochrous M8, a Biocatalyst for Production of Acrylic Heteropolymers
Grechishnikova, E. G.
Shemyakina, A. O.
Novikov, A. D.
Kalinina, T. I.
Lavrov, K. V.
Yanenko, A. S.
MICROBIOLOGY, 2024, 93 (04) : 472 - 477
[7] Nitrile hydratase and amidase from Rhodococcus rhodochrous hydrolyze acrylic fibers and granular polyacrylonitriles
Tauber, MM
Cavaco-Paulo, A
Robra, KH
Gübitz, GM
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (04) : 1634 - 1638
[8] PSEUDOMONAS-AERUGINOSA ALIPHATIC AMIDASE IS RELATED TO THE NITRILASE CYANIDE HYDRATASE ENZYME FAMILY AND CYS(166) IS PREDICTED TO BE THE ACTIVE-SITE NUCLEOPHILE OF THE CATALYTIC MECHANISM
NOVO, C
TATA, R
CLEMENTE, A
BROWN, PR
FEBS LETTERS, 1995, 367 (03) : 275 - 279
[9] Isolation of nitrile hydratase from Rhodococcus rhodochrous M8 cells and estimation of N-terminal amino acid sequences of its subunits
Sinolitskii, MK
Poltavskaya, SV
Rogacheva, SM
Sevryugina, IV
Voronin, SP
APPLIED BIOCHEMISTRY AND MICROBIOLOGY, 1997, 33 (04) : 341 - 344
[10] MONOHYDROLYSIS OF AN ALIPHATIC DINITRILE COMPOUND BY NITRILASE FROM RHODOCOCCUS-RHODOCHROUS K22
KOBAYASHI, M
YANAKA, N
NAGASAWA, T
YAMADA, H
TETRAHEDRON, 1990, 46 (16) : 5587 - 5590

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