A novel thermostable nitrilase superfamily amidase from Geobacillus pallidus showing acyl transfer activity
نویسندگان
چکیده
منابع مشابه
Structure of an aliphatic amidase from Geobacillus pallidus RAPc8.
The amidase from Geobacillus pallidus RAPc8, a moderate thermophile, is a member of the nitrilase superfamily and catalyzes the conversion of amides to the corresponding carboxylic acids and ammonia. It shows both amide-hydrolysis and acyl-transfer activities and also exhibits stereoselectivity for some enantiomeric substrates, thus making it a potentially important industrial catalyst. The cry...
متن کاملThe quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packing.
The amidase from Geobacillus pallidus RAPc8, a moderate thermophile, is a member of the nitrilase enzyme superfamily. It converts amides to the corresponding acids and ammonia and has application as an industrial catalyst. RAPc8 amidase has been cloned and functionally expressed in Escherichia coli and has been purified by heat treatment and a number of chromatographic steps. The enzyme was cry...
متن کاملCatalysis in the nitrilase superfamily.
Recently, we defined the nitrilase superfamily as consisting of 12 families of amidases, N-acyltransferases and presumptive amidases, in addition to the family of plant and bacterial nitrilases for which the superfamily was named. A novel Glu-Lys-Cys catalytic triad, found at the crystallographically defined Nit active site of worm NitFhit, was postulated to constitute the catalytic residues fo...
متن کاملCharacterization of a thermostable α-glucosidase from Geobacillus thermodenitrificans F84a
Isolation of novel thermophilic bacilli has received considerable attention among the scientific community in whole world because of their biotechnological importance as they possess unique enzymes with thermal activity and stability. Of the thermophilic enzymes, we were interested in α-glucosidases which catalyze hydrolysis of terminal non-reducing α-D-glucosidic linkages of oligoand polysacch...
متن کاملEheA from Exiguobacterium sp. yc3 is a novel thermostable DNase belonging to HNH endonuclease superfamily.
The HNH endonuclease superfamily usually contains a conserved HNH motif in the sequence, and the second subfamily of it uses N to replace the second H in the HNH motif. A bacterium with extracellular thermostable DNase was isolated and identified as Exiguobacterium sp. yc3. A 20 kDa putative DNase was later purified and the encoding gene of it was amplified and sequenced, the deduced amino acid...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Applied Microbiology and Biotechnology
سال: 2007
ISSN: 0175-7598,1432-0614
DOI: 10.1007/s00253-007-0883-2