Phase I Biotransformation Reactions-NADH-Cytochrome b5 Reductase

2007 ◽  
pp. 1-8
Author(s):  
Michael J. Barber
Keyword(s):  
Phase I ◽  
Cytochrome B5 ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome

scholarly journals Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b5 reductase from pig liver microsomes.

1987 ◽  
Vol 262 (24) ◽  
pp. 11801-11802
Author(s):  
K Miki ◽  
S Kaida ◽  
N Kasai ◽  
T Iyanagi ◽  
K Kobayashi ◽  
...  
Keyword(s):  
Cytochrome B5 ◽  
Liver Microsomes ◽  
Pig Liver ◽  
X Ray ◽  
Cytochrome B5 Reductase ◽  
Crystallographic Study ◽  
Nadh Cytochrome

Prenatal diagnosis of recessive congenital methaemoglobinaemia type II: novel mutation in the NADH-cytochrome b5 reductase gene leading to stop codon read-through

2005 ◽  
Vol 74 (5) ◽  
pp. 389-395 ◽  
Author(s):  
Alena Leroux ◽  
France Leturcq ◽  
Nathalie Deburgrave ◽  
Marie-France Szajnert
Keyword(s):  
Prenatal Diagnosis ◽  
Stop Codon ◽  
Novel Mutation ◽  
Cytochrome B5 ◽  
Type Ii ◽  
Cytochrome B5 Reductase ◽  
Reductase Gene ◽  
Nadh Cytochrome

scholarly journals Cytochrome b5 and NADH cytochrome b5 reductase: genotype–phenotype correlations for hydroxylamine reduction

2010 ◽  
Vol 20 (1) ◽  
pp. 26-37 ◽  
Author(s):  
James C. Sacco ◽  
Lauren A. Trepanier
Keyword(s):  
Cytochrome B5 ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome

scholarly journals A microplate reader-based method to quantify NADH-cytochrome b5 reductase activity for diagnosis of recessive congenital methaemoglobinemia

Hematology ◽  
2016 ◽  
Vol 22 (4) ◽  
pp. 252-257 ◽  
Author(s):  
Prabhakar Kedar ◽  
Anand Desai ◽  
Prashant Warang ◽  
Roshan Colah
Keyword(s):  
Reductase Activity ◽  
Cytochrome B5 ◽  
Cytochrome B5 Reductase ◽  
Microplate Reader ◽  
Nadh Cytochrome

Molecular Cloning of a cDNA Encoding Rat NADH-Cytochrome b5 Reductase and the Corresponding Gene1

1990 ◽  
Vol 107 (6) ◽  
pp. 810-816 ◽  
Author(s):  
Shuhei Zenno ◽  
Masahira Hattori ◽  
Yoshio Misumi ◽  
Toshitsugu Yubisui ◽  
Yoshiyuki Sakaki
Keyword(s):  
Molecular Cloning ◽  
Cytochrome B5 ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome

scholarly journals Familial Congenital Methemoglobinemia in Pomeranian Dogs Caused by a Missense Variant in the NADH-Cytochrome B5 Reductase Gene

2018 ◽  
Vol 32 (1) ◽  
pp. 165-171 ◽  
Author(s):  
H. Shino ◽  
Y. Otsuka-Yamasaki ◽  
T. Sato ◽  
K. Ooi ◽  
O. Inanami ◽  
...  
Keyword(s):  
Cytochrome B5 ◽  
Missense Variant ◽  
Cytochrome B5 Reductase ◽  
Reductase Gene ◽  
Nadh Cytochrome

A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia

Blood ◽  
2000 ◽  
Vol 95 (10) ◽  
pp. 3250-3255 ◽  
Author(s):  
Yao Wang ◽  
Yu-Shui Wu ◽  
Pei-Zhen Zheng ◽  
Wen-Xi Yang ◽  
Guo-An Fang ◽  
...  
Keyword(s):  
Clinical Symptoms ◽  
Novel Mutation ◽  
Cytochrome B5 ◽  
Clinical Manifestations ◽  
Mutant Enzyme ◽  
Chinese Family ◽  
Coding Region ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome

Abstract Recessive congenital methemoglobinemia due to nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase (b5R) deficiency is classified into 2 clinical types: type 1 (erythrocyte type) and type 2 (generalized type). We found a Chinese family with type 1 recessive congenital methemoglobinemia, the patients from which were diagnosed according to clinical symptoms and b5R enzyme activity in the blood cells. To learn the molecular basis of type 1 recessive congenital methemoglobinemia in this Chinese family, we isolated total RNA from the peripheral leukocytes of the propositus and b5R complementary DNA (cDNA) by reverse transcription– polymerase chain reaction (RT-PCR). The coding region of the b5R cDNA was analyzed by sequencing the cloned PCR products. The results showed that the propositus was homozygous for a G→A transition at codon 203 in exon 7, changing a cysteine to a tyrosine (Cys203Tyr). To characterize the mutant enzyme, both glutathione S-transferase (GST)-fused wild-type b5R and GST-fused mutant Cys203Tyr b5R were expressed in Escherichia coli and affinity purified. The results showed that the catalytic activity of the enzyme was not much affected by this amino acid substitution, but the mutant enzyme exhibited decreased heat stability and increased susceptibility to trypsin. These properties of the mutant enzyme would account for the restricted b5R deficiency and mild clinical manifestations of these type 1 patients. The finding of this novel mutation makes codon 203 the only position within the b5R gene at which more than 1 mutation has been found.

Recessive congenital methaemoglobinaemia type II, a new mutation which causes incorrect splicing in the NADH-cytochrome b5 reductase gene

1997 ◽  
Vol 20 (4) ◽  
pp. 610-610 ◽  
Author(s):  
E. P. Owen ◽  
J. Berens ◽  
A. M. Marinaki ◽  
H. Ipp ◽  
E. H. Harley
Keyword(s):  
Cytochrome B5 ◽  
Type Ii ◽  
New Mutation ◽  
Cytochrome B5 Reductase ◽  
Reductase Gene ◽  
Nadh Cytochrome
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