scholarly journals Stabilization of the Reductase Domain in the Catalytically Self-Sufficient Cytochrome P450BM3 by Consensus-Guided Mutagenesis

ChemBioChem ◽  
2018 ◽  
Vol 19 (6) ◽  
pp. 622-632 ◽  
Author(s):  
Gloria Saab-Rincón ◽  
Hanan Alwaseem ◽  
Valeria Guzmán-Luna ◽  
Leticia Olvera ◽  
Rudi Fasan
Keyword(s):  
Reductase Domain

Engineering and improvement of the efficiency of a chimeric [P450cam-RhFRed reductase domain] enzyme

2009 ◽  
pp. 2478 ◽  
Author(s):  
Aélig Robin ◽  
Gareth A. Roberts ◽  
Johannes Kisch ◽  
Federico Sabbadin ◽  
Gideon Grogan ◽  
...  
Keyword(s):  
Reductase Domain

scholarly journals Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein fromBacillus cereus

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
Heather J. Montgomery ◽  
Andrea L. Dupont ◽  
Hilary E. Leivo ◽  
J. Guy Guillemette
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Nitric Oxide Synthase ◽  
Expression And Purification ◽  
Spectral Shifts ◽  
Reconstituted System ◽  
Low Levels ◽  
And Function ◽  
Oxide Synthase ◽  
Reductase Domain

The nitric oxide synthase-like protein fromBacillus cereus(bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine andNG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation ofNG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.

scholarly journals Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor

FEBS Letters ◽  
2005 ◽  
Vol 579 (14) ◽  
pp. 3159-3163 ◽  
Author(s):  
Mónica Martínez-Moreno ◽  
Alberto Álvarez-Barrientos ◽  
Fernando Roncal ◽  
Juan Pablo Albar ◽  
Francisco Gavilanes ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Ryanodine Receptor ◽  
Endothelial Nitric Oxide Synthase ◽  
Direct Interaction ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide ◽  
Reductase Domain

Similar 150-kilobase DNA sequences are amplified in independently derived methotrexate-resistant Chinese hamster cells

1985 ◽  
Vol 5 (4) ◽  
pp. 619-627
Author(s):  
M Montoya-Zavala ◽  
J L Hamlin
Keyword(s):  
Dna Sequence ◽  
Cell Lines ◽  
Dihydrofolate Reductase ◽  
Dna Sequences ◽  
Consensus Sequence ◽  
Chinese Hamster ◽  
Ovary Cell ◽  
Chinese Hamster Cells ◽  
Reductase Gene ◽  
Reductase Domain

We have isolated overlapping recombinant cosmids that represent 150 kilobases of contiguous DNA sequence from the amplified dihydrofolate reductase domain of a methotrexate-resistant Chinese hamster ovary cell line (CHOC 400). This sequence includes the 25-kilobase dihydrofolate reductase gene and an origin of DNA synthesis. Eight cosmids that span this domain have been utilized as radioactive hybridization probes to analyze the similarities among the dihydrofolate reductase amplicons in four independently derived methotrexate-resistant Chinese hamster cell lines. We have observed no significant differences among the four cell lines within the 150-kilobase DNA sequence that we have examined, except for polymorphisms that result from the amplification of one or the other of two possible alleles of the dihydrofolate reductase domain. We also show that the restriction patterns of the amplicons in these four resistant cell lines are virtually identical to that of the corresponding, unamplified sequence in drug-susceptible parental cells. Furthermore, measurements of the relative copy numbers of fragments from widely separated regions of the amplicon suggest that all fragments in this 150-kilobase region may be amplified in unison. Our data show that in methotrexate-resistant Chinese hamster cells, the amplified unit is large relative to the dihydrofolate reductase gene itself. Furthermore, within the 150-kilobase amplified consensus sequence that we have examined, significant rearrangements do not seem to occur during the amplification process.

scholarly journals Molecular modeling of the reductase domain to elucidate the reaction mechanism of reduction of peptidyl thioester into its corresponding alcohol in non-ribosomal peptide synthetases

2010 ◽  
Vol 10 (1) ◽  
pp. 1 ◽  
Author(s):  
Balachandran Manavalan ◽  
Senthil K Murugapiran ◽  
Gwang Lee ◽  
Sangdun Choi
Keyword(s):  
Reaction Mechanism ◽  
Molecular Modeling ◽  
Peptide Synthetases ◽  
Reductase Domain

scholarly journals The Characteristics and Regulatory Mechanisms of Superoxide Generation from eNOS Reductase Domain

PLoS ONE ◽  
2015 ◽  
Vol 10 (10) ◽  
pp. e0140365 ◽  
Author(s):  
Hu Peng ◽  
Yugang Zhuang ◽  
Yuanzhuo Chen ◽  
Alicia N. Rizzo ◽  
Weiguo Chen
Keyword(s):  
Regulatory Mechanisms ◽  
Superoxide Generation ◽  
Reductase Domain

Lead Discovery of Inhibitors of the Dihydrofolate Reductase Domain ofPlasmodium falciparumDihydrofolate Reductase-Thymidylate Synthase

1997 ◽  
Vol 235 (3) ◽  
pp. 515-519 ◽  
Author(s):  
Tetsuro Toyoda ◽  
Reynolds K.B. Brobey ◽  
Gen-ichiro Sano ◽  
Toshihiro Horii ◽  
Nobuo Tomioka ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Thymidylate Synthase ◽  
Lead Discovery ◽  
Reductase Domain
Sign in / Sign up

Export Citation Format

Share Document