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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/12/29 21:57:06」(JST)
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Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids.[1] For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins.
They are usually very specific for certain amino acids. Examples of endopeptidases include:
- Trypsin - cuts after Arg or Lys, unless followed by Pro. Very strict. Works best at pH 8.
- Chymotrypsin - cuts after Phe, Trp, or Tyr, unless followed by Pro. Cuts more slowly after His, Met or Leu. Works best at pH 8.
- Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro.
- Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, unless preceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. Heat stable.
- Pepsin - cuts before Leu, Phe, Trp or Tyr, unless preceded by Pro. Also others, quite nonspecific; works best at pH 2.
- Glutamyl endopeptidase - cuts after Glu. Works best at pH 8.
- Neprilysin
References
- ^ "endopeptidase". Merriam-Webster. Archived from the original on 18 January 2017. Retrieved 18 January 2017.
External links
- Endopeptidases at the US National Library of Medicine Medical Subject Headings (MeSH)
See also
- Exopeptidase
- The Proteolysis Map
Hydrolase: proteases (EC 3.4)
|
3.4.11-19: Exopeptidase |
3.4.11 |
- Aminopeptidase
- Alanine
- Arginyl
- Aspartyl
- Cystinyl
- Leucyl
- Glutamyl
- Methionyl
- O
|
3.4.13 |
|
3.4.14 |
- Dipeptidyl peptidase
- Cathepsin C
- Dipeptidyl peptidase-4
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
- Tripeptidyl peptidase II
|
3.4.15 |
- Angiotensin-converting enzyme
|
3.4.16 |
- Serine type carboxypeptidases: Cathepsin A
- DD-transpeptidase
|
3.4.17 |
- Metalloexopeptidases
- Carboxypeptidase
- A
- A2
- B
- C
- E
- Glutamate II
|
Other/ungrouped |
|
|
3.4.21-25: Endopeptidase |
- Serine protease
- Cysteine protease
- Aspartic acid protease
- Metalloendopeptidase
- Threonine endopeptidase
- Proteasome endopeptidase complex
- HslU—HslV peptidase
- Other/ungrouped: Amyloid precursor protein secretase
- Alpha secretase
- Beta-secretase 1
- Beta-secretase 2
- Gamma secretase
|
3.4.99: Unknown |
|
Enzymes
|
Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
|
UpToDate Contents
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English Journal
- KAEA (SUDPRO), a member of the ubiquitous KEOPS/EKC protein complex, regulates the arginine catabolic pathway and the expression of several other genes in Aspergillus nidulans.
- Dzikowska A1, Grzelak A2, Gawlik J3, Szewczyk E2, Mrozek P2, Borsuk P2, Koper M2, Empel J2, Szczęsny P4, Piłsyk S5, Pękala M2, Weglenski P6.
- Gene.Gene.2015 Dec 1;573(2):310-20. doi: 10.1016/j.gene.2015.07.066. Epub 2015 Jul 23.
- The kaeA(KAE1) (suDpro) gene, which was identified in Aspergillus nidulans as a suppressor of proline auxotrophic mutations, encodes the orthologue of Saccharomyces cerevisiae Kae1p, a member of the evolutionarily conserved KEOPS/EKC (Kinase, Endopeptidase and Other Proteins of Small size/Endopeptid
- PMID 26210809
- Matrix Metalloproteinases as Regulators of Vein Structure and Function: Implications in Chronic Venous Disease.
- MacColl E1, Khalil RA2.
- The Journal of pharmacology and experimental therapeutics.J Pharmacol Exp Ther.2015 Dec;355(3):410-28. doi: 10.1124/jpet.115.227330. Epub 2015 Aug 28.
- Lower-extremity veins have efficient wall structure and function and competent valves that permit upward movement of deoxygenated blood toward the heart against hydrostatic venous pressure. Matrix metalloproteinases (MMPs) play an important role in maintaining vein wall structure and function. MMPs
- PMID 26319699
- Proteolytic processing of the streptococcal IgG endopeptidase IdeS modulates the functional properties of the enzyme and results in reduced immunorecognition.
- Persson H1, Söderberg JJ1, Vindebro R1, Johansson BP2, von Pawel-Rammingen U3.
- Molecular immunology.Mol Immunol.2015 Dec;68(2 Pt A):176-84. doi: 10.1016/j.molimm.2015.07.014. Epub 2015 Sep 3.
- The important human gram positive bacterial pathogen Streptococcus pyogenes employs various virulence factors to promote inflammation and to facilitate invasive disease progression. In this study we explored the relation of the secreted streptococcal cysteine proteases IdeS and SpeB, and neutrophil
- PMID 26343448
Japanese Journal
- 最近の心不全の臨床試験を読み解く : PARADIGM-HF試験(LCZ696)
- Microbial degradation of linear peptides by strain B-9 of Sphingosinicella and its application in peptide quantification using liquid chromatography-mass spectrometry(MISCELLANEOUS)
- Vacuolar processing enzyme in plant programmed cell death.
Related Links
- endopeptidase [en″do-pep´tĭ-dās] any peptidase that catalyzes the cleavage of internal bonds in a polypeptide or protein. Inhibition of the action of endopeptidases (proteases) in viruses causes formation of noninfectious particles ...
- Structure [edit] Prolyl endopeptidase is a cytosolic prolyl endopeptidase that cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Only short protein ...
Related Pictures
★リンクテーブル★
[★]
- 英:endopeptidase
- 関
- エキソペプチダーゼ exopeptidase、ペプチダーゼ
概念
- タンパク質の内部のペプチド鎖を加水分解しこれを断片化するペプチダーゼの総称
- トリプシン、ペプシンなど
[★]
- 英
- endopeptidase
- 関
- エンドペプチダーゼ
[★]
システインエンドペプチダーゼ
- 関
- cysteine protease、cysteine proteinase、SH protease
[★]
メタロエンドペプチダーゼ、金属エンドペプチダーゼ
- 関
- metalloendopeptidase
[★]
- 関
- 20S proteasome、proteasome
[★]
- 関
- enkephalinase、neprilysin
- 同
- NEP
[★]
PHEXリン酸調節中性エンドペプチダーゼ