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
- 関
- S-adenosylmethionine decarboxylase
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)
[Wiki en表示]
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 |
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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 |
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
This article incorporates text from the public domain Pfam and InterPro IPR003826
Carbon-carbon lyases (EC 4.1)
|
|
4.1.1: Carboxy-lyases |
- Pyruvate decarboxylase
- Oxaloacetate decarboxylase
- Acetoacetate decarboxylase
- Malonyl-CoA decarboxylase
- Glutamate decarboxylase
- Ornithine decarboxylase
- Lysine decarboxylase
- Phosphoribosylaminoimidazole carboxylase
- Histidine decarboxylase
- Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase
- Aromatic L-amino acid decarboxylase
- Phosphoenolpyruvate carboxylase
- Pyrophosphomevalonate decarboxylase
- Uroporphyrinogen III decarboxylase
- RuBisCO
- Phosphoenolpyruvate carboxykinase
- Adenosylmethionine decarboxylase
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4.1.2: Aldehyde-lyases |
- Fructose-bisphosphate aldolase
- Aldolase A
- Aldolase B
- Aldolase C
- 2-hydroxyphytanoyl-CoA lyase
- Threonine aldolase
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|
4.1.3: Oxo-acid-lyases |
- 3-hydroxy-3-methylglutaryl-CoA lyase
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|
4.1.99: Other |
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|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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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 Links
- Definition of adenosylmethionine decarboxylase in the Definitions.net dictionary. Meaning of adenosylmethionine decarboxylase. What does adenosylmethionine decarboxylase mean? Information and translations of ...
- *To whom correspondence should be addressed at the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853. Telephone: (607) 255-7961. ... S-Adenosylmethionine decarboxylase (AdoMetDC) is a ...
★リンクテーブル★
[★]
- 英
- adenosylmethionine decarboxylase
- 関
- S-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
[★]
- 英
- adenosylmethionine decarboxylase
- 関
- アデノシルメチオニン脱炭酸酵素
[★]
S-アデノシルメチオニン脱炭酸酵素、S-アデノシルメチオニンデカルボキシラーゼ
- 関
- adenosylmethionine decarboxylase
[★]
デカルボキシラーゼ、脱炭酸酵素
- 関
- carboxy-lyase
[★]