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Cofactors

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vitamin B12
vitamin involved in the metabolism of every cell
biotin
alt=3D space-filling model of Biotin rotating about an axis (GIF)|thumb|3D space-filling model of biotin rotating about an axis Biotin (also known as vitamin B7 and Vitamin H) is one of the B vitamins – a group of essential dietary micronutrients. Present in every living cell, it is involved as a cofactor for enzymes in numerous metabolic processes, both in humans and in other organisms, primarily related to the biochemistry of fats, carbohydrates, and amino acids.
vitamin B6
class of chemically related vitamins
pyridoxine
Pyridoxine (PN) is a form of vitamin B6 found commonly in food and used as a dietary supplement. As a supplement it is used to treat and prevent pyridoxine deficiency, sideroblastic anaemia, pyridoxine-dependent epilepsy, certain metabolic disorders, side effects or complications of isoniazid use, and certain types of mushroom poisoning. It is used by mouth or by injection.
heme
class=skin-invert-image|thumb|420 px|Binding of oxygen to a heme prosthetic group Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ ), is a ring-shaped iron-containing molecule that serves as a ligand of various proteins, especially as a component of hemoglobin, which carries oxygen in the bloodstream. It is composed of four pyrrole rings with two vinyl and two propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver.
cofactor
a chemical compound or metallic ion that is required for a protein's biological activity to happen
flavin adenine dinucleotide
redox cofactor, more specifically a prosthetic group, involved in several important reactions in metabolism; can exist in three (or four: flavin-N(5)-oxide) different redox states; converted between these states by accepting or donating electrons
(RS)-thioctic acid
pair of enantiomers
flavin mononucleotide
chemical compound
cyanocobalamin
Cyanocobalamin is a form of vitamin used to treat and prevent vitamin deficiency except in the presence of cyanide toxicity. The deficiency may occur in pernicious anemia, following surgical removal of the stomach, with fish tapeworm, or due to bowel cancer. It is given by mouth, by injection into a muscle, or as a nasal spray.
Coagulation factor VIII
mammalian protein found in Homo sapiens
prosthetic group
non-polypeptide unit required for the biological function of some proteins
thiamine(1+) diphosphate
chemical compound
methylcobalamin
Methylcobalamin (mecobalamin, MeCbl, or MeB) is a cobalamin, a form of vitamin B. It differs from cyanocobalamin in that the cyano group at the cobalt is replaced with a methyl group. Methylcobalamin features an octahedral cobalt(III) centre and can be obtained as bright red crystals. From the perspective of coordination chemistry, methylcobalamin is notable as a rare example of a compound that contains metal–alkyl bonds. Nickel–methyl intermediates have been proposed for the final step of methanogenesis.
pterin
Pterin is a heterocyclic compound composed of a pteridine ring system, with a "keto group" (a lactam) and an amino group on positions 4 and 2 respectively. It is structurally related to the parent bicyclic heterocycle called pteridine. Pterins, as a group, are compounds related to pterin with additional substituents. Pterin itself is of no biological significance.
cobamamide
Adenosylcobalamin (AdoCbl), also known as coenzyme B12, cobamamide, and dibencozide, is one of the biologically active forms of vitamin B12. class=skin-invert-image|left|thumb|Schematic diagram of the propionate metabolic pathway. Adenosylcobalamin is required as a coenzyme by the methylmalonyl-CoA mutase in order to convert L-methylmalonyl-CoA into succinyl-CoA, otherwise methylmalonic acid accumulates. Adenosylcobalamin participates as a cofactor in radical-mediated 1,2-carbon skeleton rearrangements. These processes require the formation of the deoxyadenosyl radical through homolytic dissoc
molybdopterin
thumb|upright=1.25|Four steps of molybdenum cofactor (Moco) biosynthetic pathway occurring in bacteria and humans: (i) radical-mediated cyclization guanosine 5'-triphosphate (GTP) to (8S)‑3,8‐cyclo‑7,8‑dihydroguanosine-5́‑triphosphate (3,8‑cH2GTP), (ii) formation of cyclic pyranopterin monophosphate (cPMP) from the 3,8‑cH2GTP, (iii) conversion of cPMP into molybdopterin (MPT), (iv) insertion of molybdate into MPT to form Moco (human enzymes in parentheses). Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. Synonyms for molybdopteri
cofactor F430
chemical compound
pyrroloquinolinedione tricarboxylic acid
chemical compound
rubredoxin
Rubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea. Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide. Like cytochromes, ferredoxins and Rieske proteins, rubredoxins are thought to participate in electron transfer in biological systems. Recent work in bacteria and algae have led to the hypothesis that some rubredoxins may instead have a role in delivering iron to metalloproteins.
SERPIND1
protein-coding gene in the species Homo sapiens
HMW kininogen
InterPro Family
L-topaquinone
Topaquinone (TPQ) is a redox cofactor derived from the amino acid tyrosine. Its name derives from 2,4,5-trihydroxyphenylalanine-quinone. Its structure was first identified in 1990. It is used by copper amine oxidases which contain a tyrosine residue near the active site. This residue catalyses its own transition, first to dopaquinone and then to topaquinone, in a Cu2+ dependent manner.