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词条 Pepsin A
释义

  1. See also

  2. References

  3. External links

{{Infobox enzyme
| Name = Pepsin A
| EC_number = 3.4.23.1
| CAS_number = 9001-75-6
| IUBMB_EC_number = 3/4/23/1
| GO_code =
| image = 1pso.jpg
| width = 270
| caption = Pepsin + inhibitor (l.blue), Human
}}Pepsin A ({{EC number|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.

See also

  • Pepsin

References

1. ^{{cite journal | vauthors = Lee D, Ryle AP | title = Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa | journal = The Biochemical Journal | volume = 104 | issue = 3 | pages = 735–41 | date = September 1967 | pmid = 4167464 | pmc = 1271213 }}
2. ^{{cite journal | vauthors = Lee D, Ryle AP | title = Pepsin D. A minor component of commercial pepsin preparations | journal = The Biochemical Journal | volume = 104 | issue = 3 | pages = 742–8 | date = September 1967 | pmid = 4860638 | pmc = 1271214 }}
3. ^{{cite journal | vauthors = Foltmann B | title = Gastric proteinases--structure, function, evolution and mechanism of action | journal = Essays in Biochemistry | volume = 17 | pages = 52–84 | date = 1981 | pmid = 6795036 }}
4. ^{{cite journal | vauthors = James MN, Sielecki AR | title = Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution | journal = Nature | volume = 319 | issue = 6048 | pages = 33–8 | date = 1986 | pmid = 3941737 | doi = 10.1038/319033a0 }}
5. ^{{cite book | chapter = Aspartyl proteinases | title = New Comprehensive Biochemistry: Hydrolytic Enzymes |author1 = Fruton, J.S. |date = 1987 |volume = 16 |pages = 1–38 |editor = Neuberger, A. |author2 =Brocklehurst, K. |edition = |publisher = Elsevier |location = Amsterdam }}
6. ^{{cite journal | vauthors = Tang J, Wong RN | title = Evolution in the structure and function of aspartic proteases | journal = Journal of Cellular Biochemistry | volume = 33 | issue = 1 | pages = 53–63 | date = January 1987 | pmid = 3546346 | doi = 10.1002/jcb.240330106 }}
7. ^{{cite journal | vauthors = Pohl J, Dunn BM | title = Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site | journal = Biochemistry | volume = 27 | issue = 13 | pages = 4827–34 | date = June 1988 | pmid = 3139029 | doi = 10.1021/bi00413a037 }}

External links

  • {{MeshName|Pepsin+A}}
{{Aspartic acid proteases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}

1 : EC 3.4.23

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