scholarly journals In silico Analysis and Molecular Modelling of NADH-cytochrome b5 Reductase 3 involved in Methemoglobinemia

2020 ◽  
pp. 229-233
Author(s):  
Someshwar C. M. Moholkar ◽  
Mamta S. Kongari ◽  
Shubhangi S. Sakhare
Keyword(s):  
Cytochrome B5 ◽  
3D Structure ◽  
Alpha Helix ◽  
In Silico Analysis ◽  
Cytochrome B5 Reductase ◽  
Random Coils ◽  
Validation Score ◽  
Nadh Cytochrome ◽  
Tools And Techniques ◽  
Genetic Form

Methemoglobinemia is type of disease caused due to methemoglobin. Methemoglobin is type of hemoglobin in which the iron heme3+ is present instead of fe2+. Normally methemoglobin is present in every living cell, but if it is present in large amount then it will responsible for causing disease. Acquired methemoglobinemia known as acute methemoglobinemia caused by exposure of medicines, chemicals, foods. People suffering from genetic form have higher chances of developing acquired type. Most cases of acquired methemoglobinemia result from exposure to certain drugs or toxins. In the present study we have used different Insilico tools and techniques which are includes retrieval of NADH-cytochrome b5 reductase 3protein sequence from the UniProt KB database and physicochemical parameter analyzed by using Protoparam tool. In that Leucine had a maximum amino acid composition. The structure of a protein has a very important role in its function. The secondary structure was predicted by using SOPMA tool which indicated that the percentage of Random coils was higher than the percentage of alpha helix and extended strand. Then the 3D structure of b5 reductase 3 was predicted by using SWISS MODEL server and the model was validated by using PROCHECK analysis after validation of the model, the validation score was 94.7%.

scholarly journals Serine-proline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type

Blood ◽  
1990 ◽  
Vol 75 (7) ◽  
pp. 1408-1413 ◽  
Author(s):  
Y Kobayashi ◽  
Y Fukumaki ◽  
T Yubisui ◽  
J Inoue ◽  
Y Sakaki
Keyword(s):  
Cytochrome B5 ◽  
Alpha Helix ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Enzyme Deficiency ◽  
Nucleotide Binding Domain ◽  
Lymphoblastoid Cells ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome ◽  
Generalized Type

Hereditary methemoglobinemia is an autosomal recessive disorder characterized by NADH-cytochrome b5 reductase (b5R) deficiency. In an attempt to clarify the molecular mechanisms involved in the enzyme deficiency, we isolated the b5R gene from a patient homozygous for hereditary methemoglobinemia, generalized type, and compared its nucleotide sequence with that of the normal NADH-cytochrome b5R gene. Only one difference was observed; a thymidine at the first position of codon 127 (TCT) was altered to a cytidine in the b5R gene of the patient, resulting in replacement of serine with proline. Dot blot hybridization of the amplified DNA samples with allele-specific oligonucleotide probes showed that the proband and her brothers were homozygous for this mutation and that their father was heterozygous. Although the activity of b5R in lymphoblastoid cells from homozygotes was reduced to 10% of the normal level, RNA blot and protein blot analyses of the lymphoblastoid cells showed that synthesis of b5R messenger RNA and the b5R polypeptide were normal. Serine at residue 127 is presumed to be in an alpha-helix structure that is part of a nucleotide-binding domain. These observations suggest that replacement of Pro-127 causes a significant conformation change in the nucleotide- binding domain that affects electron transport from NADH to cytochrome b5. Functional enzyme deficiency results in a generalized type of hereditary methemoglobinemia.

scholarly journals Serine-proline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type

Blood ◽  
1990 ◽  
Vol 75 (7) ◽  
pp. 1408-1413 ◽  
Author(s):  
Y Kobayashi ◽  
Y Fukumaki ◽  
T Yubisui ◽  
J Inoue ◽  
Y Sakaki
Keyword(s):  
Cytochrome B5 ◽  
Alpha Helix ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Enzyme Deficiency ◽  
Nucleotide Binding Domain ◽  
Lymphoblastoid Cells ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome ◽  
Generalized Type

Abstract Hereditary methemoglobinemia is an autosomal recessive disorder characterized by NADH-cytochrome b5 reductase (b5R) deficiency. In an attempt to clarify the molecular mechanisms involved in the enzyme deficiency, we isolated the b5R gene from a patient homozygous for hereditary methemoglobinemia, generalized type, and compared its nucleotide sequence with that of the normal NADH-cytochrome b5R gene. Only one difference was observed; a thymidine at the first position of codon 127 (TCT) was altered to a cytidine in the b5R gene of the patient, resulting in replacement of serine with proline. Dot blot hybridization of the amplified DNA samples with allele-specific oligonucleotide probes showed that the proband and her brothers were homozygous for this mutation and that their father was heterozygous. Although the activity of b5R in lymphoblastoid cells from homozygotes was reduced to 10% of the normal level, RNA blot and protein blot analyses of the lymphoblastoid cells showed that synthesis of b5R messenger RNA and the b5R polypeptide were normal. Serine at residue 127 is presumed to be in an alpha-helix structure that is part of a nucleotide-binding domain. These observations suggest that replacement of Pro-127 causes a significant conformation change in the nucleotide- binding domain that affects electron transport from NADH to cytochrome b5. Functional enzyme deficiency results in a generalized type of hereditary methemoglobinemia.

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
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