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carboxyglutamic acid
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carboxyglutamic acid
please note:
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{{Chembox| ImageFile = Carboxyglutamic acid.svg| ImageSize =| SystematicName = 3-Aminopropane-1,1,3-tricarboxylic acid| OtherNames = γ-Carboxyglutamate|Section1={{Chembox Identifiers| ChemSpiderID = 37241| InChI = 1/C6H9NO6/c7-3(6(12)13)1-2(4(8)9)5(10)11/h2-3H,1,7H2,(H,8,9)(H,10,11)(H,12,13)| InChIKey = UHBYWPGGCSDKFX-UHFFFAOYAH- the content below is remote from Wikipedia
- it has been imported raw for GetWiki
correct|CAS}}| CASNo=53861-57-7 | correct|FDA}}| UNII = 16FQV4RZKL| PubChem=40772| SMILES = O=C(O)C(C(=O)O)CC(N)C(=O)O}}|Section2={{Chembox Properties| Formula=C6H9NO6| MolarMass=191.14 g/mol| Appearance=| Density=1.649 g/mL| MeltingPt=| BoilingPtC=418| Solubility=
}}|Section3={{Chembox Hazards| MainHazards=| FlashPt=| AutoignitionPt =
}}Carboxyglutamic acid (or the conjugate base, carboxyglutamate), is an uncommon amino acid introduced into proteins by a post-translational carboxylation of glutamic acid residues. This modification is found, for example, in clotting factors and other proteins of the coagulation cascade. This modification introduces an affinity for calcium ions. In the blood coagulation cascade, vitamin K is required to introduce γ-carboxylation of clotting factors II, VII, IX, X and protein Z.JOURNAL, Vitamin Kâdependent formation of γ-carboxyglutamic acid, Annual Review of Biochemistry}} | pages = 157â172 | pmid = 332061 | year = 1977, SynthesisIn the biosynthesis of γ-carboxyglutamic acid, the γ-proton on glutamic acid is abstracted, and CO2 is subsequently added. The reaction intermediate is a γ-glutamyl carbanion.This reaction is catalyzed by a carboxylase that requires vitamin K as its cofactor. It is not exactly known how vitamin K participates, but it is hypothesized that a free cysteine residue in the carboxylase converts vitamin K into an active strong base that in turn abstracts a hydrogen from glutamic acid’s γ-carbon. Then CO2 is added to the γ-carbon to form γ-carboxyglutamic acid.JOURNAL, Vitamin Kâdependent biosynthesis of γ-carboxyglutamic acid,www.bloodjournal.org/content/93/6/1798, Blood, 1999-03-15, 0006-4971, 10068650, 1798â1808, 93, 6, en, Bruce, Furie, Beth A., Bouchard, Barbara C., Furie, 10.1182/blood.V93.6.1798.406k22_1798_1808,γ-Carboxyglutamic acid-rich (GLA) domainA number of γ-carboxyglutamate residues are present in the γ-carboxyglutamic acid-rich (“GLA“) domain. This GLA domain is known to be found in over a dozen known proteins, including coagulation factors X, VII, IX, and XIV, vitamin K-dependent protein S and Z, prothrombin, transthyretin, osteocalcin, matrix Gla protein (MGP), inter-alpha trypsin inhibitor heavy chain H2, and growth arrest-specific protein 6 (GAS6). The Gla domain is responsible for high-affinity binding of calcium ions (Ca2+) to Gla proteins, which is often necessary for their conformation, and always necessary for their function.WEB, Gamma-carboxyglutamic acid-rich (GLA) domain (IPR000294) | < InterPro < EMBL-EBI,www.ebi.ac.uk/interpro/entry/IPR000294, www.ebi.ac.uk, 2015-12-22,