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
WordNet
- the 19th letter of the Roman alphabet (同)s
- any of the enzymes that hydrolize the carboxyl group
PrepTutorEJDIC
- sulfurの化学記号 / {略}South[ern]
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/09 15:52:26」(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 |
|
| 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; PDBj |
| 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)
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|
| 4.1.1: Carboxy-lyases |
- Acetoacetate decarboxylase
- Adenosylmethionine decarboxylase
- Aromatic L-amino acid decarboxylase
- Glutamate decarboxylase
- Histidine decarboxylase
- Lysine decarboxylase
- Malonyl-CoA decarboxylase
- Ornithine decarboxylase
- Oxaloacetate decarboxylase
- Phosphoenolpyruvate carboxykinase
- Phosphoenolpyruvate carboxylase
- Phosphoribosylaminoimidazole carboxylase
- Pyrophosphomevalonate decarboxylase
- Pyruvate decarboxylase
- RuBisCO
- Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase
- Uroporphyrinogen III decarboxylase
|
|
| 4.1.2: Aldehyde-lyases |
- Fructose-bisphosphate aldolase
- Aldolase A
- Aldolase B
- Aldolase C
- 2-hydroxyphytanoyl-CoA lyase
- Threonine aldolase
|
|
| 4.1.3: Oxo-acid-lyases |
- Isocitrate lyase
- 3-hydroxy-3-methylglutaryl-CoA lyase
|
|
| 4.1.99: Other |
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|
|
Enzymes
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|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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|
UpToDate Contents
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English Journal
- Arginase 2 deletion leads to enhanced M1 macrophage activation and upregulated polyamine metabolism in response to Helicobacter pylori infection.
- Hardbower DM1,2, Asim M2, Murray-Stewart T3, Casero RA Jr3, Verriere T2, Lewis ND2, Chaturvedi R2,4, Piazuelo MB2, Wilson KT5,6,7,8,9.
- Amino acids.Amino Acids.2016 Apr 13. [Epub ahead of print]
- We reported that arginase 2 (ARG2) deletion results in increased gastritis and decreased bacterial burden during Helicobacter pylori infection in mice. Our studies implicated a potential role for inducible nitric oxide (NO) synthase (NOS2), as Arg2 -/- mice exhibited increased NOS2 levels in gastric
- PMID 27074721
- Cotton S-adenosylmethionine decarboxylase-mediated spermine biosynthesis is required for salicylic acid- and leucine-correlated signaling in the defense response to Verticillium dahliae.
- Mo HJ1, Sun YX2, Zhu XL1, Wang XF1, Zhang Y1, Yang J1, Yan GJ1,3, Ma ZY4.
- Planta.Planta.2016 Apr;243(4):1023-39. doi: 10.1007/s00425-015-2463-5. Epub 2016 Jan 13.
- MAIN CONCLUSION: Cotton S-adenosylmethionine decarboxylase-, rather than spermine synthase-, mediated spermine biosynthesis is required for salicylic acid- and leucine-correlated signaling in the defense response to Verticillium dahliae. Spermine (Spm) signaling is correlated with plant resistance t
- PMID 26757733
- Effect of polyamines on the grain filling of wheat under drought stress.
- Liu Y1, Liang H2, Lv X2, Liu D2, Wen X2, Liao Y3.
- Plant physiology and biochemistry : PPB / Société française de physiologie végétale.Plant Physiol Biochem.2016 Mar;100:113-29. doi: 10.1016/j.plaphy.2016.01.003. Epub 2016 Jan 14.
- Drought inhibits wheat grain filling. Polyamines (PAs) are closely associated with plant resistance due to drought and grain filling of cereals. However, little is known about the effect of PAs on the grain filling of wheat under drought stress. This study investigated whether and how PAs are involv
- PMID 26812255
Japanese Journal
- Conformational Stabilization of Rat S-Adenosylmethionine Decarboxylase by Putrescine
- Identification of the Primary Structure and Post-translational Modification of Rat S-Adenosylmethionine Decarboxylase
- Conformational Stabilization of Rat S-Adenosylmethionine Decarboxylase by Putrescine
Related Links
- 1. Essays Biochem. 2009 Nov 4;46:25-45. doi: 10.1042/bse0460003. S-Adenosylmethionine decarboxylase. Pegg AE. Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey ...
- Adenosylmethionine Decarboxylase; S-Adenosylmethionine Decarboxylase. On-line free medical diagnosis assistant. Ranked list of possible diseases from either several symptoms or a full patient history. A similarity measure ...
★リンクテーブル★
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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
[★]
- 英
- S-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デカルボキシラーゼ
[★]
- 英
- S-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
[★]
デカルボキシラーゼ、脱炭酸酵素
- 関
- carboxy-lyase
[★]
[★]