ペプシンA
- 関
- pepsin
WordNet
- the 1st letter of the Roman alphabet (同)a
- the blood group whose red cells carry the A antigen (同)type_A, group A
- an enzyme produced in the stomach that splits proteins into peptones
PrepTutorEJDIC
- answer / ampere
- ペプシン(胃液中の蛋白質分解酵素) / ペプシン剤,消化剤
- arsenicの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/21 16:00:52」(JST)
[Wiki en表示]
| Pepsin A |
| Identifiers |
| EC number |
3.4.23.1 |
| CAS number |
9001-75-6 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
Pepsin A (EC 3.4.23.1, pepsin, lactated pepsin, pepsin fortior, fundus-pepsin, elixir lactate of pepsin, P I, lactated pepsin elixir, P II, pepsin R, pepsin D) is an enzyme.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1-Val, Gln4-His, Glu13-Ala, Ala14-Leu, Leu15-Tyr, Tyr16-Leu, Gly23-Phe, Phe24-Phe and Phe25-Tyr bonds in the B chain of insulin
The enzyme is a predominant endopeptidase in the gastric juice of vertebrates.
References[edit]
- ^ Lee, D. and Ryle, A.P. (1967). "Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa". Biochem. J. 104: 735–741. PMID 4167464.
- ^ Lee, D. and Ryle, A.P. (1967). "Pepsin D. A minor component of commercial pepsin preparations". Biochem. J. 104: 742–748. PMID 4860638.
- ^ Foltmann, R. (1981). "Gastric proteinases -structure, function, evolution and mechanism of action". Essays Biochem. 17: 52–84. PMID 6795036.
- ^ James, M.N.G. and Sielecki, A.R. (1986). "Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution". Nature 319: 33–38. PMID 3941737.
- ^ Fruton, J.S. (1987). "Aspartyl proteinases". In Neuberger, A. and Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes 16. Amsterdam: Elsevier. pp. 1–38.
- ^ Tang, J. and Wong, R.N.S. (1987). "Evolution in the structure and function of aspartic proteases". J. Cell. Biochem. 33: 53–63. PMID 3546346.
- ^ Pohl, J. and Dunn, B.M. (1988). "Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site". Biochemistry 27: 4827–4834. PMID 3139029.
See also[edit]
External links[edit]
- Pepsin A at the US National Library of Medicine Medical Subject Headings (MeSH)
UpToDate Contents
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English Journal
- Effects of temperature, pH and sugar binding on the structures of lectins ebulin f and SELfd.
- Carrillo C1, Cordoba-Diaz D2, Cordoba-Diaz M2, Girbés T3, Jiménez P1.
- Food chemistry.Food Chem.2017 Apr 1;220:324-330. doi: 10.1016/j.foodchem.2016.10.007. Epub 2016 Oct 4.
- Ebulin f and SELfd are two lectins of Sambucus ebulus L. that show different stability and digestibility properties in gastric fluid due to their structural differences which may explain their different toxicological profiles. The main aim was to determine the effects of pH, temperature and sugar bi
- PMID 27855907
- Designing dairy desserts for weight management: Structure, physical properties and in vitro gastric digestion.
- Borreani J1, Llorca E2, Quiles A3, Hernando I4.
- Food chemistry.Food Chem.2017 Apr 1;220:137-144. doi: 10.1016/j.foodchem.2016.09.202. Epub 2016 Sep 30.
- The first aim of this study was to observe the effect of adding dairy proteins and reducing the cream content in order to obtain healthier dairy desserts for use in weight management. The extra-whey protein low-cream sample had the densest, firmest matrix, which is related to increased satiety. The
- PMID 27855881
- Impact of the environmental conditions and substrate pre-treatment on whey protein hydrolysis: A review.
- Cheison SC1, Kulozik U2.
- Critical reviews in food science and nutrition.Crit Rev Food Sci Nutr.2017 Jan 22;57(2):418-453.
- Proteins in solution are subject to myriad forces stemming from interactions with each other as well as with the solvent media. The role of the environmental conditions, namely pH, temperature, ionic strength remains under-estimated yet it impacts protein conformations and consequently its interacti
- PMID 25976220
Japanese Journal
- 小豆子葉部のα-グルコシダーゼ活性およびGLP-1分泌に与える影響
- 濱岡 直裕,中川 良二,比良 徹 [他]
- 日本食品科学工学会誌 = Journal of the Japanese Society for Food Science and Technology 60(1), 43-47, 2013-01-00
- NAID 40019543735
- 佐藤 里絵
- 日本食品化学学会誌 19(3), 172-177, 2012-12-21
- … Mutations of Cys65 and Cys66 in rFag e 2 decreased the pepsin digestibility of the protein, and an ELISA inhibition assay revealed a weaker inhibitory effect of rFag e 2 C65S than that of rFag e 2 WT. …
- NAID 110009561743
- Purification, gene cloning and characterization of an acidic β-1,4-glucanase from Phialophora sp. G5 with potential applications in the brewing and feed industries(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Zhao Junqi,Shi Pengjun,Yuan Tiezheng,Huang Huoqing,Li Zhongyuan,Meng Kun,Yang Peilong,Yao Bin
- Journal of bioscience and bioengineering 114(4), 379-384, 2012-10-00
- … The enzyme showed some properties superior than most fungal β-1,4-glucanases, such as high activity over a wide pH range (exhibiting >50% of the maximum activity at pH 2.0-7.0), excellent stability in extreme acidic to alkaline conditions (pH 2.0-9.0), and strong resistance against pepsin and trypsin (retaining 89% and 94% activity, respectively). …
- NAID 110009543720
★リンクテーブル★
[★]
- 英
- pepsin A
- 関
- ペプシン
[★]
[★]
- 関
- adenoviral、adenovirus