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Binding of AdoMet to its enzyme AdoMetDC is the first step and binding occurs through the pyruvate prosthetic group, reacting to give a Schiff base <ref name="six"/>. The pyruvate then acts as an election sink, helping to break the carbon to carboxylic acid bond (C-COO-) resulting in a carbon dioxide (CO2) being eliminated <ref name="six"/>. Protonation occurs at the R carbon of the product resulting in the release of dcAdoMet <ref name="six"/>. This protonation also regenerates the pyruvate cofactor so that it is available and ready for another reaction <ref name="six"/>.
Binding of AdoMet to its enzyme AdoMetDC is the first step and binding occurs through the pyruvate prosthetic group, reacting to give a Schiff base <ref name="six"/>. The pyruvate then acts as an election sink, helping to break the carbon to carboxylic acid bond (C-COO-) resulting in a carbon dioxide (CO2) being eliminated <ref name="six"/>. Protonation occurs at the R carbon of the product resulting in the release of dcAdoMet <ref name="six"/>. This protonation also regenerates the pyruvate cofactor so that it is available and ready for another reaction <ref name="six"/>.
==References==
==References==
<refernces/>
<references/>
1. Tolbert WD, Ekstrom JL, Mathews II, Secrist JA, Kapoor P, Pegg AE, Ealick SE. The structural basis for substrate specificity and inhibition of human S-Adenosylmethionine decarboxylase. Biochem. 2001 Jun 21;40:9484-94.
 
2.Xiong H, Stanley BA, Tekwani BL, Pegg AE. Processing of mammalian and plant S-Adenosylmethionine decarboxylase proenzymes. J Biological Chem. 1997 Mar 11;272(45):28342-48.
 
3.Ekstrom JL, Tolbert WD, Xiong H, Pegg AE, Ealick SE. Structure of a human S-Adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant. Biochem. 2001Jun 5;40(32):9495-504.
 
4.Tolbert WD, Zhang Y, Cottet SE, Bennett EM, Ekstrom JL, Pegg AE, Ealick SE. Mechanism of human S-Adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant. Biochem. 2003 Feb 7;42(8):2386-95.
 
5.Bale S, Brooks W, Hans JW, Mahesan AM, Guida WC, Ealick SE. Role of the sulfonium center in determining the ligand specificity of human S-Adenosylmethionine decarboxylase. Biochem. 2009 Jun 15;48(27):6423-30.
 
6.Xiong H, Stanley BA, Pegg AE. Role of cysteine-82 in the catalytic mechanism of human S-Adenosylmethionine. Biochem. 1999 Feb 4;38(8):2462-70.

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