scholarly journals Purification and Characterization of Cholesterol Oxidase from Novel Sources –Aspergillus awamori and Aspergillus fumigatus

2019 ◽  
Vol 08 (04) ◽  
pp. 345-354
Author(s):  
Majumder Devipriya ◽  
Yelpure Chetna ◽  
FarhaNaaz Abdul Wajid ◽  
Syed Nagma
2008 ◽  
Vol 7 (4) ◽  
pp. 751-756 ◽  
Author(s):  
M.T. Yazdi ◽  
Z.T. Yazdi ◽  
A. Ghasemian ◽  
G. Zarrini ◽  
N.H. Olyaee ◽  
...  

1961 ◽  
Vol 14 (4) ◽  
pp. 347-358 ◽  
Author(s):  
Evelyn M. Rau ◽  
Evelyn B. Tilden ◽  
Virgil L. Koenig

Microbiology ◽  
2005 ◽  
Vol 151 (7) ◽  
pp. 2199-2207 ◽  
Author(s):  
Alexander Grundmann ◽  
Shu-Ming Li

A putative prenyltransferase gene, ftmPT1, was identified in the genome sequence of Aspergillus fumigatus. ftmPT1 was cloned and expressed in Escherichia coli, and the protein FtmPT1 was purified to near homogeneity and characterized biochemically. This enzyme was found to catalyse the prenylation of cyclo-l-trp-l-Pro (brevianamide F) at the C-2 position of the indole nucleus. FtmPT1 is a soluble monomeric protein, which does not contain the usual prenyl diphosphate binding site (N/D)DXXD found in most prenyltransferases, and which does not require divalent metal ions for its enzymic activity. K m values for brevianamide F and dimethylallyl diphosphate were determined as 55 and 74 μM, respectively. The turnover number was 5·57 s−1. FtmPT1 showed a high substrate specificity towards dimethylallyl diphosphate, but accepted different tryptophan-containing cyclic dipeptides. Together with dimethylallyltryptophan synthase of ergot alkaloid biosynthesis, FtmPT1 belongs to a new group of prenyltransferases with aromatic substrates.


2013 ◽  
Vol 170 (4) ◽  
pp. 895-908 ◽  
Author(s):  
Raja Tahir Mahmood ◽  
Muhammad Javaid Asad ◽  
Nazia Mehboob ◽  
Maria Mushtaq ◽  
Muhammad Gulfraz ◽  
...  

2021 ◽  
Vol 0 (0) ◽  
pp. 0-0
Author(s):  
Ashraf El-Sayed ◽  
Mostafa G. Ali ◽  
Reyad El-Sharkawy ◽  
Nesma El-sayed ◽  
Mahmoud Amer

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