Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Protein Variants

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 18 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3G811V site-directed mutagenesis, an FAD-binding mutant 742843
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3H654A/H677A site-directed mutagenesis, CD spectroscopy shows no negative effects of the introduced mutations on protein secondary structure in comparison to the wild-type protein, but the mutant contains no heme, while the FAD binding ability is not significantly disturbed 742843
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more construction of null-mutants of gene niaD 655066
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more different structural gene (niaD) and cofactor gene (cnx) mutants are analyzed concerning their flavin and molybdenum content 395973
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more nit-1 mutant, suggested to produce the complete apoenzyme 395978
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more nit-1 mutant: lacks all activities except FAD-dependent NADPH:cytochrome c reductase activity,nit-2 mutant: reduced FAD:- and reduced methyl viologen:nitrate reductase activities but lacks the other two activities 395980
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more nit-3 mutant (FGSC 262): reduced FAD-nitrate reductase and reduced methylviologen-nitrate reductase activities 395981
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more several mutations of recombinant cyt b reductase fragment of nitrate reductase in the region Ser920, Arg921 and Arg932 are created. Conversion from NADPH-specific to virtually NADH-specific cyt b reductase fragment of nitrate reductase 395976
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more studies of temperature-sensitive mutations, niaD gene: mutation leads to loss of a 4.5-S cytochrome-c reductase activity, which is a subunit of nitrate reductase. It is suggested that neither the product of the cnxE nor the cnyF genes form part of the nitrate reductase molecule, but some catalytic role in cofactor formation, niaD and cnxH seem to be structural genes -, 395967
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.3more the purified native enzyme is successfully used for synthesis of silver nanoparticles in an NADPH-dependent manner using gelatin as a capping agent, analysis by X-ray diffraction, dynamic light scattering spectroscopy, and transmission and scanning electron microscopy, overview. 0.2 M Phosphate buffer, pH 7.2, 1 mM silver nitrate as the enzyme substrate, 0.1 mg gelatin as a capping agent, 1 mM 4-hydroxyquinoline as an electron carrier, 1 mM NADPH as enzyme cofactor, and 0.1 mg of purified fungal nitrate reductase are incubated at 25°C for 5 h. The stable nonaggregating nanoparticles are spherical in shape with an average size of 50 nm and a zeta potential of -34.3. The synthesized nanoparticles show a strong growth inhibitory antimicrobial activity against all tested human pathogenic fungi and bacteria, overview -, 741637
Results 1 - 10 of 18 > >>