Thermostable hydantoinase from a hyperthermophilic archaeon, Methanococcus jannaschii

被引：12

作者：

Chung, JH

Back, JH

Lim, JH

Park, YI

Han, YS

机构：

[1] Korea Inst Sci & Technol, Struct Biol Res Ctr, Seoul 130650, South Korea

[2] Korea Univ, Grad Sch Biotechnol, Seoul 136701, South Korea

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2002年 / 30卷 / 07期

关键词：

hydantoinase; hyperthermophile; Methanococcus jannaschii; stereospecificity; thermostability;

D O I：

10.1016/S0141-0229(02)00047-9

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A hyperthermophilic hydantoinase from Methanococcus jannaschii with an optimum growth at 85degreesC was cloned and expressed in E. coli. The recombinant,hydantoinase was petrified by affinity and anion-exchange chromatography and determined to be homotetrameric protein by gel filtration chromatography. The best substrate for the hydantoinase was D,L-5-hydroxyhydantoin, which has the specific activity of 183.4 U/mg. The optimum pH and temperature for the hydantoinase activity was 8.0 and 80degreesC, respectively. The half-life of the hydantoinase was measured to be 100 min at 90degreesC in the buffer containing 500 mM KCl. Manganese ions were the most effective for the hydantoinase activity. Stereospecificity was determined to be L-specific for the 5-hydroxymethylhydantoin and 5-methylhydantoin by chiral TLC. The activity yields as well as the operational stabilities of the thermostable M. jannaschii hydantoinase could be significantly improved by immobilization method. (C) 2002 Elsevier Science Inc. All rights reserved.

引用

页码：867 / 874

页数：8

共 39 条

[1] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].

Altschul, SF ;

Madden, TL ;

Schaffer, AA ;

Zhang, JH ;

Zhang, Z ;

Miller, W ;

Lipman, DJ .

NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402

[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii [J].

Bult, CJ ;

White, O ;

Olsen, GJ ;

Zhou, LX ;

Fleischmann, RD ;

Sutton, GG ;

Blake, JA ;

FitzGerald, LM ;

Clayton, RA ;

Gocayne, JD ;

Kerlavage, AR ;

Dougherty, BA ;

Tomb, JF ;

Adams, MD ;

Reich, CI ;

Overbeek, R ;

Kirkness, EF ;

Weinstock, KG ;

Merrick, JM ;

Glodek, A ;

Scott, JL ;

Geoghagen, NSM ;

Weidman, JF ;

Fuhrmann, JL ;

Nguyen, D ;

Utterback, TR ;

Kelley, JM ;

Peterson, JD ;

Sadow, PW ;

Hanna, MC ;

Cotton, MD ;

Roberts, KM ;

Hurst, MA ;

Kaine, BP ;

Borodovsky, M ;

Klenk, HP ;

Fraser, CM ;

Smith, HO ;

Woese, CR ;

Venter, JC .

SCIENCE, 1996, 273 (5278) :1058-1073

[4] The complete genome of the hyperthermophilic bacterium Aquifex aeolicus [J].

Deckert, G ;

Warren, PV ;

Gaasterland, T ;

Young, WG ;

Lenox, AL ;

Graham, DE ;

Overbeek, R ;

Snead, MA ;

Keller, M ;

Aujay, M ;

Huber, R ;

Feldman, RA ;

Short, JM ;

Olsen, GJ ;

Swanson, RV .

NATURE, 1998, 392 (6674) :353-358

[5]

Drauz K., 1995, ENZYME CATALYSIS ORG

[6] PROPERTIES OF D-HYDANTOINASE FROM AGROBACTERIUM-TUMEFACIENS AND ITS USE FOR THE PREPARATION OF N-CARBAMYL D-AMINO ACIDS [J].

DURHAM, DR ;

WEBER, JE .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1995, 216 (03) :1095-1100

[7] Formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - New insights into salt-dependence and thermostability [J].

Ermler, U ;

Merckel, MC ;

Thauer, RK ;

Shima, S .

STRUCTURE, 1997, 5 (05) :635-646

[8] METHANOCOCCUS-JANNASCHII SP-NOV, AN EXTREMELY THERMOPHILIC METHANOGEN FROM A SUBMARINE HYDROTHERMAL VENT [J].

JONES, WJ ;

LEIGH, JA ;

MAYER, F ;

WOESE, CR ;

WOLFE, RS .

ARCHIVES OF MICROBIOLOGY, 1983, 136 (04) :254-261

[9]

Kawarabayasi Y, 1999, DNA Res, V6, P83, DOI 10.1093/dnares/6.2.83

[10] Primary structure, sequence analysis, and expression of the thermostable D-hydantoinase from Bacillus stearothermophilus SD1 [J].

Kim, GJ ;

Park, JH ;

Lee, DC ;

Ro, HS ;

Kim, HS .

MOLECULAR & GENERAL GENETICS, 1997, 255 (02) :152-156

← 1 2 3 4 →