WordNet

any of the enzymes that hydrolize the carboxyl group

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/04/22 16:32:25」(JST)

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AdoMet decarboxylase

crystal structure of thermotoga maritima s-adenosylmethionine decarboxylase

Identifiers

Symbol

AdoMet_dc

Pfam

PF02675

InterPro

IPR003826

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Adenosylmethionine decarboxylase is an enzyme that catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine. Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in a large number of cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein.^[1]^[2] Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. In both groups the active enzyme is generated by the post-translational autocatalytic cleavage of a precursor protein. This cleavage generates the pyruvate precursor from an internal serine residue and results in the formation of two non-identical subunits termed alpha and beta which form the active enzyme.

References

^ van Poelje PD, Snell EE (1990). "Pyruvoyl-dependent enzymes". Annu. Rev. Biochem. 59: 29–59. doi:10.1146/annurev.bi.59.070190.000333. PMID 2197977.
^ Pegg AE, Xiong H, Feith DJ, Shantz LM (November 1998). "S-adenosylmethionine decarboxylase: structure, function and regulation by polyamines". Biochem. Soc. Trans. 26 (4): 580–6. PMID 10047786.

External links

Reaction: R00178

This article incorporates text from the public domain Pfam and InterPro IPR003826

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English Journal

Trypanosoma brucei S-adenosylmethionine decarboxylase N-terminus is essential for allosteric activation by the regulatory subunit prozyme.

Velez N, Brautigam CA, Phillips MA.SourceUniv of Texas SW Medical Ctr, United States.
The Journal of biological chemistry.J Biol Chem.2013 Jan 3. [Epub ahead of print]
Human African trypanosomiasis (HAT) is caused by a single-celled protozoan parasite, Trypanosoma brucei. Polyamine biosynthesis is a clinically validated target for the treatment of HAT. Metabolic differences between the parasite and the human polyamine pathway are thought to contribute to species s
PMID 23288847

Selective regulation of nicotine and polyamines biosynthesis in tobacco cells by enantiomers of ornithine.

Gholami M, Fakhari AR, Ghanati F.SourceMedicinal Plants and Drugs Research Institute (MPDRI), Shahid Beheshti University, G.C., Tehran, Iran. m_gholami@sbu.ac.ir.
Chirality.Chirality.2013 Jan;25(1):22-7. doi: 10.1002/chir.22107. Epub 2012 Sep 19.
l- and d-amino acids have diverse functions and effects on the metabolism, growth, and development of plants. Ornithine (Orn) plays a main role in the biosynthesis of many amino acids, nicotinic alkaloids, and polyamines in tobacco. This investigation describes the impact of Orn enantiomers on the p
PMID 22996307

Effects of promoter methylation on increased expression of polyamine biosynthetic genes in suicide.

Gross JA, Fiori LM, Labonté B, Lopez JP, Turecki G.SourceMcGill Group for Suicide Studies, Douglas Mental Health University Institute, McGill University, 6875 boul. Lasalle, Verdun, Quebec H4H 1R3, Canada.
Journal of psychiatric research.J Psychiatr Res.2012 Dec 19. pii: S0022-3956(12)00358-5. doi: 10.1016/j.jpsychires.2012.11.016. [Epub ahead of print]
Suicide is among the leading causes of death worldwide. The polyamine system has been increasingly implicated in the neurobiology of suicide. Previous research has indicated that epigenetic mechanisms play a role in explaining dysregulation of polyamine genes in suicide completers. Nevertheless, reg
PMID 23260169

Japanese Journal

Conformational Stabilization of Rat S-Adenosylmethionine Decarboxylase by Putrescine

Wada Makiko,Shirahata Akira
Biological & Pharmaceutical Bulletin 33(11), 1800-1805, 2010
… The activity and processing of mammalian S-adenosylmethionine decarboxylase (AdoMetDC) is stimulated by putrescine. …
NAID 130000402299

Identification of the Primary Structure and Post-translational Modification of Rat S-Adenosylmethionine Decarboxylase

Wada Makiko,Shirahata Akira
Biological & Pharmaceutical Bulletin 33(5), 891-894, 2010
… The coding region nucleotide sequences of rat, hamster, and bovine S-adenosylmethionine decarboxylase (AdoMetDC) cDNA exhibit over 90% homology with the human sequence. …
NAID 130000248054

Related Pictures

★リンクテーブル★

リンク元	「アデノシルメチオニン脱炭酸酵素」「アデノシルメチオニンデカルボキシラーゼ」
拡張検索	「S-adenosylmethionine decarboxylase」
関連記事	「decarboxylase」「adenosylmethionine」

「アデノシルメチオニン脱炭酸酵素」

adenosylmethionine decarboxylase 1
Identifiers
Symbol	AMD1
Entrez	262
HUGO	457
OMIM	180980
RefSeq	NM_001634
UniProt	P17707
Other data
EC number	4.1.1.50
Locus	Chr. 6 q21-q22

Search
PMC	articles
PubMed	articles
NCBI	proteins

adenosylmethionine decarboxylase
Identifiers
EC number	4.1.1.50
CAS number	9036-20-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins