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Titolo:
Structural basis for cold adaptation - Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum
Autore:
Kim, SY; Hwang, KY; Kim, SH; Sung, HC; Han, YS; Cho, YJ;
Indirizzi:
Korea Inst Sci & Technol, Struct Biol Ctr, Seoul 130650, South Korea KoreaInst Sci & Technol Seoul South Korea 130650 ul 130650, South Korea Korea Univ, Dept Biotechnol, Seoul, South Korea Korea Univ Seoul South Korea Univ, Dept Biotechnol, Seoul, South Korea Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 pt Chem, Berkeley, CA 94720 USA Univ Calif Berkeley, Lawrence Berkeley Lab, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 ley Lab, Berkeley, CA 94720 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 17, volume: 274, anno: 1999,
pagine: 11761 - 11767
SICI:
0021-9258(19990423)274:17<11761:SBFCA->2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVE CITRATE SYNTHASE; ESCHERICHIA-COLI; LACTATE-DEHYDROGENASE; ANTARCTIC BACTERIUM; RESOLUTION; ENZYMES; THERMOSTABILITY; PURIFICATION; EXPRESSION; STABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Cho, YJ Koreaeanst Sci & Technol, Struct Biol Ctr, POB 131, Seoul 130650, South Kor Korea Inst Sci & Technol POB 131 Seoul South Korea 130650 uth Kor
Citazione:
S.Y. Kim et al., "Structural basis for cold adaptation - Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum", J BIOL CHEM, 274(17), 1999, pp. 11761-11767

Abstract

Aquaspillium arcticum is a psychrophilic bacterium that was isolated from arctic sediment and grows optimally at 4 degrees C, We have cloned, purified, and characterized malate dehydrogenase from A. arcticum (Aa MDH). We also have determined the crystal structures of apo-Aa MDH, Aa MDH.NADH binary complex, and Aa MDH.NAD.oxaloacetate ternary complex at 1.9-, 2.1-, and 2.5-Angstrom resolutions, respectively. The Aa MDH sequence is most closely related to the sequence of a thermophilic MDH from Thermus flavus (Tf MDH), showing 61% sequence identity and over 90% sequence similarity. Stability studies show that Aa MDH has a half-life of 10 min at 55 degrees C, whereas Tf MDH is fully active at 90 degrees C for 1 h. Aa MDH shows 2-3-fold highercatalytic efficiency compared with a mesophilic or a thermophilic MDH at the temperature range 4-10 degrees C. Structural comparison of Aa MDH and TfMDH suggests that the increased relative flexibility of active site residues, favorable surface charge distribution for substrate and cofactor, and the reduced intersubunit ion pair interactions may be the major factors for the efficient catalytic activity of Aa MDH at low temperatures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 06:50:45