Limited Proteolysis of Thermostable Alanine Racemase of Bacillus stearothermophilus.
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چکیده
منابع مشابه
Thermostable a-Amylase of Bacillus stearothermophilus
Some general and physical properties and the’ amino acid composition of the thermostable cr-amylase of Bacillus sbarothermophilus have been described in previous papers (l-3). In an effort to further correlate the thermostability of this enzyme with its molecular organization, a study of the structure of this protein has been undertaken. In this paper are reported the results of an investigatio...
متن کاملCulture Conditions for Production of Thermostable Amylase by Bacillus stearothermophilus.
Bacillus stearothermophilus grew better on complex and semisynthetic medium than on synthetic medium supplemented with amino acids. Amylase production on the complex medium containing beef extract or corn steep liquor was higher than on semisynthetic medium containing peptone (0.4%). The synthetic medium, however, did not provide a good yield of extracellular amylase. Among the carbohydrates wh...
متن کاملCloning and Expression of Thermostable alpha-Amylase Gene from Bacillus stearothermophilus in Bacillus stearothermophilus and Bacillus subtilis.
The structural gene for a thermostable alpha-amylase from Bacillus stearothermophilus was cloned in plasmids pTB90 and pTB53. It was expressed in both B. stearothermophilus and Bacillus subtilis. B. stearothermophilus carrying the recombinant plasmid produced about fivefold more alpha-amylase (20.9 U/mg of dry cells) than did the wild-type strain of B. stearothermophilus. Some properties of the...
متن کاملThermostable, Raw-Starch-Digesting Amylase from Bacillus stearothermophilus.
An endospore-forming thermophilic bacterium, which produced amylase and was identified as Bacillus stearothermophilus, was isolated from soil. The amylase had an optimum temperature of 70 degrees C and strongly degraded wheat starch granules (93%) and potato starch granules (80%) at 60 degrees C.
متن کاملReaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine.
The crystal structures of alanine racemase bound with reaction intermediate analogs, N-(5'-phosphopyridoxyl)-L-alanine (PLP-L-Ala) and N-(5'-phosphopyridoxyl)-D-alanine (PLP-D-Ala), were determined at 2.0-A resolution with the crystallographic R factor of 17.2 for PLP-L-Ala and 16.9 for PLP-D-Ala complexes. They were quite similar not only to each other but also to the structure of the native p...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1991
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.55.2881