Cobamide

Last updated
Cobamide
Cobamide.png
Cobamide.gif
Names
IUPAC name
cobalt;[(2R,3S,4R,5S)-4,5-dihydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2R)-1-[3-[(1R,2R,3R,4Z,7S,9Z,12S,13S,14Z,17S,18S,19R)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2,7,12,17-tetrahydro-1H-corrin-21-id-3-yl]propanoylamino]propan-2-yl] hydrogen phosphate
Identifiers
  • 14709-02-5
3D model (JSmol)
ChEBI
KEGG
PubChem CID
  • InChI=1S/C53H82N11O15P.Co/c1-24(78-80(75,76)79-44-32(23-65)77-48(74)43(44)73)22-60-40(72)16-17-50(6)30(18-37(57)69)47-53(9)52(8,21-39(59)71)29(12-15-36(56)68)42(64-53)26(3)46-51(7,20-38(58)70)27(10-13-34(54)66)31(61-46)19-33-49(4,5)28(11-14-35(55)67)41(62-33)25(2)45(50)63-47;/h19,24,27-30,32,43-44,47-48,65,73-74H,10-18,20-23H2,1-9H3,(H15,54,55,56,57,58,59,60,61,62,63,64,66,67,68,69,70,71,72,75,76);/p-1/t24-,27-,28-,29-,30+,32-,43-,44-,47-,48+,50-,51+,52+,53+;/m1./s1
    Key: WUZNOFXZJICPCQ-NHIUFCJESA-M
  • CC1=C2C(C(C([N-]2)C3(C(C(C(=N3)C(=C4C(C(C(=N4)C=C5C(C(C1=N5)CCC(=O)N)(C)C)CCC(=O)N)(C)CC(=O)N)C)CCC(=O)N)(C)CC(=O)N)C)CC(=O)N)(C)CCC(=O)NCC(C)OP(=O)(O)OC6C(OC(C6O)O)CO.[Co]
Properties
C53H81CoN11O15P
Molar mass 1202.200 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

Cobamide is a naturally occurring chemical compound containing cobalt in the corrinoid family of macrocyclic complexes. Cobamide works as a coenzyme with some enzymes in bacteria. The cobalt atom may have a transferable methyl group attached. It is used for example in 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase. [1] [2]


Related Research Articles

Oxidative phosphorylation The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.

Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing the chemical energy stored within the nutrients in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.

Metalloprotein Protein that contains a metal ion cofactor

Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.

Thiocyanate Ion

Thiocyanate is the anion [SCN]−. It is the conjugate base of thiocyanic acid. Common derivatives include the colourless salts potassium thiocyanate and sodium thiocyanate. Organic compounds containing the functional group SCN are also called thiocyanates. Mercury(II) thiocyanate was formerly used in pyrotechnics.

Bioinorganic chemistry is a field that examines the role of metals in biology. Bioinorganic chemistry includes the study of both natural phenomena such as the behavior of metalloproteins as well as artificially introduced metals, including those that are non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins.

Corrinoid

Corrinoids are a group of compounds based on the skeleton of corrin, a cyclic system containing four pyrrole rings similar to porphyrins. These include compounds based on octadehydrocorrin, which has the trivial name corrole.

In enzymology, nitrile hydratases are mononuclear iron or non-corrinoid cobalt enzymes that catalyse the hydration of diverse nitriles to their corresponding amides

In enzymology, a tetrachloroethene reductive dehalogenase is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family.

In enzymology, a CoB—CoM heterodisulfide reductase (EC 1.8.98.1) is an enzyme that catalyzes the chemical reaction

Cob(I)yrinic acid a,c-diamide adenosyltransferase

In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.

Cobalamin biosynthesis

Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.

5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase is an enzyme with systematic name 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein methyltransferase. This enzyme catalyses the following chemical reaction:

(Methyl-Co methanol-specific corrinoid protein):coenzyme M methyltransferase is an enzyme with systematic name methylated methanol-specific corrinoid protein:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction

(Methyl-Co methylamine-specific corrinoid protein):coenzyme M methyltransferase is an enzyme with systematic name methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction

Methylamine-corrinoid protein Co-methyltransferase is an enzyme with systematic name monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Dimethylamine-corrinoid protein Co-methyltransferase is an enzyme with systematic name dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Trimethylamine-corrinoid protein Co-methyltransferase is an enzyme with systematic name trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Methylated-thiol-coenzyme M methyltransferase is an enzyme with systematic name methylated-thiol:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction:

5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase is an enzyme with systematic name 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase. This enzyme catalyses the following chemical reaction

Lawrence Que Jr. is a chemist who specializes in bioinorganic chemistry and is a Regents Professor at the University of Minnesota, Twin Cities. He received the 2017 American Chemical Society (ACS) Award in Inorganic Chemistry for his contributions to the field., and the 2008 ACS Alfred Bader Award in Bioinorganic Chemistry.

Julia A. Kovacs is an American chemist specializing in bioinorganic chemistry. She is Professor of Chemistry at the University of Washington. Her research involves synthesizing small-molecule mimics of the active sites of metalloproteins, in order to investigate how cysteinates influence the function of non-heme iron enzymes, and the mechanism of the oxygen-evolving complex (OEC).

References

  1. ↑ Maupin-Furlow, J.; Ferry, J.G. (1996). "Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila". J. Bacteriol. 178 (2): 340–346. doi:10.1128/jb.178.2.340-346.1996. PMC   177663 . PMID   8550451.
  2. ↑ Grahame, D.A.; DeMoll, E. (1996). "Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri". J. Biol. Chem. 271 (14): 8352–8358. doi: 10.1074/jbc.271.14.8352 . PMID   8626532.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.