Information about Methemoglobin Reductase

Ribbon diagram of erythrocytic methemoglobin reductase with FAD bound. From PDB 1UMK.
cytochrome b5 reductase 3
Identifiers
SymbolCYB5R3
Alt. SymbolsDIA1
Entrez1727
HUGO2873
OMIM250800
PDB1UMK
RefSeqNM_007326
UniProtP00387
Other data
EC number1.6.2.2
LocusChr. 22 q13.31-qter
Methemoglobin reductase (also known as cytochrome-b5 reductase) is an enzyme which converts methemoglobin to hemoglobin.

See also

External links

Red blood cells are the most common type of blood cell and the vertebrate body's principal means of delivering oxygen from the lungs or gills to body tissues via the blood.
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In biochemistry, flavin adenine dinucleotide (FAD) is the precursor molecule to FADH2. Upon bonding to two hydrogen atoms, FAD is then changed to FADH2 and is turned into an energy-carrying molecule.
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Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. This data, typically obtained by X-ray crystallography or NMR spectroscopy, is submitted by biologists and biochemists from around the world, is released into the public domain,
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The Entrez Global Query Cross-Database Search System is a powerful federated search engine, or web portal that allows users to search many discrete health sciences databases at the National Center for Biotechnology Information (NCBI) website.
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Hugo is a male given name, a latinized form of the name Hugh, a German/Teutonic name meaning "Bright in Mind and Spirit".

Hugo is one of the most popular names in Europe ranking as high as #2 in France, #6 in Spain, and #7 in Belgium in 2006.
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Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. This data, typically obtained by X-ray crystallography or NMR spectroscopy, is submitted by biologists and biochemists from around the world, is released into the public domain,
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The National Center for Biotechnology Information (NCBI) is part of the United States National Library of Medicine (NLM), a branch of the National Institutes of Health. The NCBI is located in Bethesda, Maryland and was founded in 1988.
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Swiss-Prot is a manually curated biological database of protein sequences. Swiss-Prot was created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute.
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Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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locus (plural loci) is a fixed position on a chromosome, such as the position of a gene or a biomarker (genetic marker). A variant of the DNA sequence at a given locus is called an allele. The ordered list of loci known for a particular genome is called a genetic map.
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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Methemoglobin (pronounced MET-hemoglobin) is a form of the oxygen-carrying protein hemoglobin (British English: haemoglobin), in which the iron in the heme group is in the Fe3+ state, not the Fe2+ of normal hemoglobin. Methemoglobin is unable to carry oxygen.
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Hemoglobin, also spelled haemoglobin and abbreviated Hb, is the iron-containing oxygen-transport metalloprotein in the red blood cells of the blood in vertebrates and other animals.
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Methemoglobinemia
Classification & external resources

ICD-10 D 74.
ICD-9 289.7

DiseasesDB 8100

eMedicine med/1466   emerg/313
MeSH D008708

Methemoglobinemia
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A reductase is an enzyme which lowers the activation energy for a reduction reaction. [1][2]

Examples

  • 5-alpha reductase
  • Dihydrofolate reductase
  • HMG-CoA reductase
  • Methemoglobin reductase
  • Ribonucleotide reductase

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Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed
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Nicotinamide adenine dinucleotide (NAD+ or in older notation DPN+) is an important coenzyme found in cells. It plays key roles as a carrier of electrons and a participant in metabolic redox reactions, as well as in cell signaling.
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Nicotinamide adenine dinucleotide phosphate (NADP) is used in anabolic reactions, such as fatty acid and nucleic acid synthesis, which require NADPH as a reducing agent.

NADPH is the reduced form of NADP+, and NADP+ is the oxidized form of NADPH.
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In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydrogen acceptor or electron donor) to another (the oxidant, also called the hydrogen donor or electron acceptor).
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Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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The NADPH oxidase (nicotinamide adenine dinucleotide phosphate-oxidase) complex is an enzyme complex

Subunits

It is made up of six subunits. These subunits are:

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P91-PHOX is a glycoprotein associated with chronic granulomatous disease.

External link

  • MeSH gp91phox+protein,+human


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NADH dehydrogenase (EC 1.6.5.3 ) is an enzyme located in the inner mitochodrial membrane that catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). It is also called the NADH:quinone oxidoreductase.
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).

Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence,
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The acetolactate synthase (ALS) enzyme (also known as acetohydroxyacid synthase, or AHAS) is the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine).
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Acyl CoA dehydrogenase is the enzyme used to catalyze the first step of β-oxidation in Fatty acid metabolism.

Reaction

The following reaction is the oxidation of the fatty acid by FAD.

The enzyme catalyzes the formation of a double bond between the C-2 and C-3.
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Apoptosis inducing factor is a flavoprotein.

See also

  • Apoptosis

External links

  • MeSH Apoptosis+inducing+factor


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Butyryl CoA dehydrogenase is a flavoprotein.

It acts upon butyryl-coenzyme A.

See also

  • Butyric_acid#Butyrate_fermentation
  • Causes_of_hypoglycemia#Metabolic_Defects

External links

  • MeSH Butyryl-CoA+Dehydrogenase

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Identifiers
Symbol CRY2

Entrez 1408
HUGO 2385
OMIM 603732

RefSeq NM_021117
UniProt Q49AN0
Other data

Locus Chr. 11 p11.2 Cryptochrome is a name used historically for the blue light photoreceptors of plants.
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