NDLI: Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

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Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

Year: 1998 Volume: 7 Issue: 4

Year: 1998 Volume: 7 Issue: 3

Year: 1998 Volume: 7 Issue: 2

Year: 1998 Volume: 7 Issue: 1

Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Frolow, F. Burstein, Y. Kalb(Gilboa), A. J. Bogin, O. Korkhin, Y. Peretz, M. Hacham, Y.
Description	Country affiliation: Israel Author Affiliation: Bogin O ( Department of Organic Chemistry, The Weizmann Institute of Science, Rehovot, Israel.)
Abstract	A comparison of the three-dimensional structures of the closely related mesophilic Clostridium beijerinckii alcohol dehydrogenase (CBADH) and the hyperthermophilic Thermoanaerobacter brockii alcohol dehydrogenase (TBADH) suggested that extra proline residues in TBADH located in strategically important positions might contribute to the extreme thermal stability of TBADH. We used site-directed mutagenesis to replace eight complementary residue positions in CBADH, one residue at a time, with proline. All eight single-proline mutants and a double-proline mutant of CBADH were enzymatically active. The critical sites for increasing thermostability parameters in CBADH were Leu-316 and Ser-24, and to a lesser degree, Ala-347. Substituting proline for His-222, Leu-275, and Thr-149, however, reduced thermal stability parameters. Our results show that the thermal stability of the mesophilic CBADH can be moderately enhanced by substituting proline at strategic positions analogous to nonconserved prolines in the homologous thermophilic TBADH. The proline residues that appear to be crucial for the increased thermal stability of CBADH are located at a beta-turn and a terminating external loop in the polypeptide chain. Positioning proline at the N-caps of alpha-helices in CBADH led to adverse effects on thermostability, whereas single-proline mutations in other positions in the polypeptide had varying effects on thermal parameters. The finding presented here support the idea that at least two of the eight extra prolines in TBADH contribute to its thermal stability.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	7
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1998-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alcohol Dehydrogenase Metabolism Bacteria, Anaerobic Enzymology Clostridium Gram-positive Asporogenous Rods, Irregular Proline Chemistry Amino Acid Sequence Amino Acid Substitution Enzyme Stability Molecular Sequence Data Sequence Homology, Amino Acid Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

Enhanced thermal stability ofClostridium beijerinckiialcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilicThermoanaerobacter brockiialcohol dehydrogenase

Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.

Oligomeric integrity--the structural key to thermal stability in bacterial alcohol dehydrogenases.

PROTEINS: Structure, Function, and Bioinformatics 66:196–204 (2007) A Single Proline Substitution is Critical for the Thermostabilization of Clostridium beijerinckii Alcohol Dehydrogenase

Cysteine reactivity in Thermoanaerobacter brockii alcohol dehydrogenase.

Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.

A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase.

Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging.

Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

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