DOI: 10.1002/jcb.240330106. Evolution in the structure and function of aspartic proteases

Evolution in the structure and function of aspartic proteases

10.1002/jcb.240330106

Crossref journal-article

Wiley

Journal of Cellular Biochemistry (311)

Abstract

AbstractAspartic proteases (EC3.4.23) are a group of proteolytic enzymes of the pepsin family that share the same catalytic apparatus and usually function in acid solutions. This latter aspect limits the function of aspartic proteases to some specific locations in different organisms; thus the occurrence of aspartic proteases is less abundant than other groups of proteases, such as serine proteases. The best known sources of aspartic proteases are stomach (for pepsin, gastricsin. and chymosin). lysosomes (for cathepsins D and E), kidney (for renin), yeast granules, and fungi (for secreted proteases such as rhizopuspepsin, penicillopepsin, and endothiapepsin). These aspartic proteases have been extensively studied for their structure and function relationships and have been the topics of several reviews or monographs (Tang: Acid Proteases, Structure, Function and Biology. New York: Plenum Press, 1977; Tang: J Mol Cell Biochem 26:93–109, 1979; Kostka: Aspartic Proteinases and Their Inhibitors. Berlin: Walter de Gruyter, 1985). All mammalian aspartic proteases are synthesized as zymogens and are subsequently activated to active proteases. Although a zymogen for a fungal aspartic protease has not been found, the cDNA structure of rhizopuspepsin suggests the presence of a “pro” enzyme (Wong et al: Fed Proc 44:2725, 1985). It is probable that other fungal aspartic proteases are also synthesized as zymogens.It is the aim of this article to summarize the major models of structure‐function relationships of aspartic proteases and their zymogens with emphasis on more recent findings. Attempts will also be made to relate these models to other aspartic proteases.

Bibliography

Tang, J., & Wong, R. N. S. (1987). Evolution in the structure and function of aspartic proteases. Journal of Cellular Biochemistry, 33(1), 53â63. Portico.

Authors 2

Jordan Tang (first)
Ricky N. S. Wong (additional)

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Dates

Type	When
Created	20 years, 7 months ago (Dec. 30, 2004, 10:18 a.m.)
Deposited	1 year, 10 months ago (Oct. 21, 2023, 6:36 a.m.)
Indexed	3 weeks, 4 days ago (July 30, 2025, 8:24 p.m.)
Issued	38 years, 7 months ago (Jan. 1, 1987)
Published	38 years, 7 months ago (Jan. 1, 1987)
Published Online	21 years, 6 months ago (Feb. 19, 2004)
Published Print	38 years, 7 months ago (Jan. 1, 1987)

Funders 0

None

BibTeX

@article{Tang_1987, title={Evolution in the structure and function of aspartic proteases}, volume={33}, ISSN={1097-4644}, url={http://dx.doi.org/10.1002/jcb.240330106}, DOI={10.1002/jcb.240330106}, number={1}, journal={Journal of Cellular Biochemistry}, publisher={Wiley}, author={Tang, Jordan and Wong, Ricky N. S.}, year={1987}, month=jan, pages={53–63} }

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