エキソペプチダーゼ、ペプチド末端加水分解酵素
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/22 10:06:19」(JST)
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An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain. Depending on whether the amino acid is released from the amino or the carboxy terminal, an exopeptidase is further classified as an aminopeptidase or a carboxypeptidase, respectively. Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.
See also
- The Proteolysis Map
- Endopeptidase
- Edman degradation
- Dansyl chloride
- Protease
External links
- Exopeptidases at the US National Library of Medicine Medical Subject Headings (MeSH)
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Hydrolase: proteases (EC 3.4)
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| 3.4.11-19: Exopeptidase |
| 3.4.11 |
- Aminopeptidase
- Alanine
- Arginyl
- Aspartyl
- Cystinyl
- Leucyl
- Glutamyl
- Methionyl
- O
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| 3.4.13 |
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| 3.4.14 |
- Dipeptidyl peptidase
- Cathepsin C
- Dipeptidyl peptidase-4
- Tripeptidyl peptidase
- Tripeptidyl peptidase I
- Tripeptidyl peptidase II
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| 3.4.15 |
- Angiotensin-converting enzyme
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| 3.4.16 |
- Serine type carboxypeptidases: Cathepsin A
- DD-transpeptidase
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| 3.4.17 |
- Metalloexopeptidases
- Carboxypeptidase
- A
- A2
- B
- C
- E
- Glutamate II
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| Other/ungrouped |
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| 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
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| 3.4.99: Unknown |
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Proteins: 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
- Purification and biochemical characterization of dipeptidyl peptidase-II (DPP7) homologue from germinated Vigna radiata seeds.
- Khaket TP1, Dhanda S2, Jodha D2, Singh J3.
- Bioorganic chemistry.Bioorg Chem.2015 Dec;63:132-41. doi: 10.1016/j.bioorg.2015.10.004. Epub 2015 Oct 22.
- Dipeptidyl peptidases (DPPs) are potent exopeptidases, which possess central role in proteolysis. As compared to other members of DPP family, proline containing dipeptide hydrolysing activity of DPP-II (Dipeptidyl peptidase II) is unique as it hydrolyses imino group and plays a key role in protein m
- PMID 26524724
- Inhibition of endopeptidase and exopeptidase activity of cathepsin B impairs extracellular matrix degradation and tumour invasion.
- Mitrović A, Mirković B, Sosič I, Gobec S, Kos J.
- Biological chemistry.Biol Chem.2015 Nov 13. pii: /j/bchm.just-accepted/hsz-2015-0236/hsz-2015-0236.xml. doi: 10.1515/hsz-2015-0236. [Epub ahead of print]
- Cathepsin B is a lysosomal cysteine protease that is implicated in a number of physiological processes, including protein turnover in lysosomes. Changes in its expression are associated with a variety of pathological processes, including cancer. Due to the structural feature, termed the occluding lo
- PMID 26565553
- Cysteine-Rich Peptide Family with Unusual Disulfide Connectivity from Jasminum sambac.
- Kumari G1, Serra A1, Shin J1, Nguyen PQ1, Sze SK1, Yoon HS1, Tam JP1.
- Journal of natural products.J Nat Prod.2015 Nov 10. [Epub ahead of print]
- Cysteine-rich peptides (CRPs) are natural products with privileged peptidyl structures that represent a potentially rich source of bioactive compounds. Here, the discovery and characterization of a novel plant CRP family, jasmintides from Jasminum sambac of the Oleaceae family, are described. Two 27
- PMID 26555361
Japanese Journal
- X線結晶構造解析による新規エキソペプチダーゼの分子機構解明 (特集 バイオマーカー探索を指向した先端的薬学研究(その2))
- 昭和学士会雑誌 = Journal of the Showa University Society 75(3), 296-301, 2015-06
- NAID 40020659059
- A Missing Link Between a High Salt Intake and Blood Pressure Increase
- Journal of pharmacological sciences 100(5), 370-390, 2006-05-15
- NAID 10018238332
- Exopeptidase Degradation for the Analysis of Phosphorylation Site in a Mono-phosphorylated Peptide with Matrix-assisted Laser Desorption/Ionization Mass Spectrometry
- Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 19(11), 1469-1472, 2003-11-10
- NAID 10012533839
Related Links
- exopeptidase / ˌɛk soʊˈpɛp tɪˌdeɪs, -ˌdeɪz / Show Spelled [ek-soh-pep-ti-deys, -deyz] Show IPA noun Biochemistry. any enzyme that catalyzes the removal of an amino acid from the end of a polypeptide chain. Compare endopeptidase
- exopeptidase /exo·pep·ti·dase/ (-pep´tĭ-dās) any peptidase that catalyzes the cleavage of the terminal or penultimate peptide bond, releasing a single amino acid or dipeptide from the peptide chain. ex·o·pep·ti·dase (k s-p p t-d s, -d z)
★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:exopeptidase
-カルボキシペプチダーゼA、カルボキシペプチダーゼB
- 英
- [[]]
- 同
- exopeptidase
- 英
- exopeptidase
- 同
- exopeptidase
[★]
- 英
- exopeptidase
- 関
- エキソペプチダーゼ
[★]
メタロエキソペプチダーゼ