Aspartic proteinases in fishes and aquatic invertebrates.
1. The literature on molecular properties and physiological role of aspartic proteinases in fishes and aquatic invertebrates has been reviewed. 2. Pepsins have not been detected in invertebrates, and apparently cathepsin D, as well as other cathepsins, act both as digestive and lysosomal enzymes in many of these animals. The molecular properties of invertebrate cathepsin D correspond with cathepsin D in fishes and mammalians. 3. Fishes with a true stomach have pepsinogen secretion. Fish pepsins have higher pH optimum and are less stable in strong acid conditions than mammalian pepsins. They are very efficient at low temperatures, but less thermostable than mammalian pepsins. 4. Many fishes have two significantly different pepsins: Pepsin I and Pepsin II, which digest haemoglobin at a maximal rate in the pH ranges 3-4 and 2-3 respectively. Usually the pI of Pepsin I is in the range 6.5-7, whereas pI of Pepsin II is about 4. 5. Fish Pepsin I and cathepsin D have very similar molecular properties, and a hypothesis proposing that cathepsin D is the ancestor enzyme of aspartic proteinases in higher animals is presented.
Gildberg
A
A
Institute of Fishery Technology Research, Tromsø, Norway.
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D / Q000502:physiology; D010450:Endopeptidases / Q000266:history / Q000502:physiology*; D005399:Fishes; D049672:History, 19th Century; D049673:History, 20th Century; D007448:Invertebrates; D008386:Marine Biology; D010434:Pepsin A / Q000502:physiology
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A; D002402:Cathepsin D