Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: S-adenosylmethionine decarboxylase

Gene: AMD1 Accession Number: HS04667 (MetaCyc)

Synonyms: G-9018, AMD

Species: Homo sapiens

Subunit composition of S-adenosylmethionine decarboxylase = [S-adenosylmethionine decarboxylase α subunit]2[S-adenosylmethionine decarboxylase β subunit]2

Summary:
S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme for the biosynthesis of polyamines and is one of a small class of enzymes that use a covalently bound pyruvoyl prosthetic group. The pyruvoyl group is thought to act analogously to pyridoxal phosphate cofactor by forming a Schiff base with the amino group of the substrate and then serving as an electron sink to facilitate the decarboxylation [Diaz91].

Four of these enzymes, histidine decarboxylase (E.C. 4.1.1.22), phosphatidylserine decarboxylase, aspartate 1-decarboxylase, and S-adenosylmethionine decarboxylase are decarboxylases forming important biological amines. All of these enzymes are known to have the pyruvoyl prosthetic group attached via an amide linkage to the amino terminus of the α subunit. Two other enzymes in this group are are D-proline reductase and glycine reductase (E.C. 1.21.4.2) [Xiong99].

Pyruvoyl-containing enzymes are expressed as a zymogen which is processed post-translationally by a self-maturation cleavage called serinolysis. In this process the pyruvoul group is formed from a serine residue, splitting the presursor protein into two parts which become the α and β subunits. In some cases additional subunits may be involved.

S-adenosylmethionine decarboxylase is a short lived enzyme. The enzyme is deactivated by substrate-mediated transamination, which is followed by rapid ubiquination and degradation by the 26 S proteasome [Kolar52].

Gene Citations: [Pajunen88]

Map Position: [111,218,852 -> 111,239,777]

Molecular Weight: 38 kD (experimental) [Stanley89 ]

Unification Links: Entrez-gene:262

Gene-Reaction Schematic: ?


Enzymatic reaction of: S-adenosylmethionine decarboxylase

Synonyms: AdoMetDC, SamDC

EC Number: 4.1.1.50

S-adenosyl-L-methionine + H+ <=> CO2 + S-adenosyl 3-(methylthio)propylamine

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of polyamine biosynthesis II , methionine salvage cycle III (animals) , spermine biosynthesis , spermidine biosynthesis I


Subunit of S-adenosylmethionine decarboxylase: S-adenosylmethionine decarboxylase α subunit

Gene: AMD1 Accession Number: HS04667 (MetaCyc)

Sequence Length: 20923/3 AAs

Molecular Weight: 30.7 kD (experimental) [Stanley89]

Relationship Links: UniProt:PART-OF:P17707


Subunit of S-adenosylmethionine decarboxylase: S-adenosylmethionine decarboxylase β subunit

Gene: AMD1 Accession Number: HS04667 (MetaCyc)

Sequence Length: 20923/3 AAs

Molecular Weight: 7.7 kD (experimental) [Stanley89]

Relationship Links: UniProt:PART-OF:P17707

Exons/Introns:

History:
10/31/2011 (caspi) Merged genes G-9018/AMD1 into HS04667/AMD1


References

Diaz91: Diaz E, Anton DL (1991). "Alkylation of an active-site cysteinyl residue during substrate-dependent inactivation of Escherichia coli S-adenosylmethionine decarboxylase." Biochemistry 1991;30(16);4078-81. PMID: 2018773

Ekstrom99: Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE (1999). "The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold." Structure Fold Des 7(5);583-95. PMID: 10378277

Kolar52: Kolar, V (1952). "[Experiences with the treatment of leukemia.]." Bratisl Lek Listy 7(2);38-42. PMID: 14918534

Pajunen88: Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE (1988). "Structure and regulation of mammalian S-adenosylmethionine decarboxylase." J Biol Chem 263(32);17040-9. PMID: 2460457

Stanley89: Stanley BA, Pegg AE, Holm I (1989). "Site of pyruvate formation and processing of mammalian S-adenosylmethionine decarboxylase proenzyme." J Biol Chem 264(35);21073-9. PMID: 2687270

Xiong99: Xiong H, Pegg AE (1999). "Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate." J Biol Chem 274(49);35059-66. PMID: 10574985


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, BIOCYC14B.