Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1
نویسندگان
چکیده
منابع مشابه
Production and Purification of d-Aminoacylase from Alcaligenes denitrificans and Taxonomic Study of the Strain.
A d-aminoacylase-producing microorganism, strain DA181, isolated from soil was identified as Alcaligenes denitrificans subsp. denitrificans. This strain produced about 29,300 units (micromoles of product formed per hour) of d-aminoacylase and 2,300 units of l-aminoacylase per gram of cells (wet weight) when cultivated in a medium containing 1% N-acetyl-dl-leucine as the carbon source. The d-ami...
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The purification and initial characterization of arsenite oxidase from Alcaligenes faecalis are described. The enzyme consists of a monomer of 85 kDa containing one molybdenum, five or six irons, and inorganic sulfide. In the presence of denaturants arsenite oxidase releases a fluorescent material with spectral properties identical to the pterin cofactor released by the hydroxylase class of mol...
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D-Aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) was strongly inactivated by diethylpyrocarbonate (DEPC). An H67N mutant was barely active, with a kcat/Km 6.3 x 10(4) times lower than that of the recombinant wild-type enzyme, while the H67I mutant lost detectable activity. The H67N mutant had almost constant Km, but greatly decreased kcat. These results sug...
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Aromatic amine dehydrogenase was purified and characterized from Alcaligenes xylosoxidans IFO13495 grown on beta-phenylethylamine. The molecular mass of the enzyme was 95.5 kDa. The enzyme consisted of heterotetrameric subunits (alpha2beta2) with two different molecular masses of 42.3 kDa and 15.2 kDa. The N-terminal amino acid sequences of the alpha-subunit (42.3-kDa subunit) and the beta-subu...
متن کاملPurification and characterization of a novel 5-oxoprolinase (without ATP-hydrolyzing activity) from Alcaligenes faecalis N-38A.
A novel type of 5-oxoprolinase was found in a cell extract of strain N-38A, which was later identified as Alcaligenes faecalis. The enzyme in the cell extract was purified to a homogeneous state with a yield of 16.6%. The molecular weight of the purified enzyme was estimated to be 47,000 by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, suggesting that the en...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1991
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.57.4.1259-1260.1991