Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species.
Abstract: The kinetic parameters Km, k+2 and k+2/Km of the pancreatic ribonucleases (EC 3.1.4.22) from cow, giraffe, horse, rat and lesser rorqual have been determined, using 2',3'-cyclic cytidine monophosphate and 2',3'-cuclic uridine monophosphate as substrates. No large differences were found between the activities of the five enzymes. The relative differences between the activities of the five enzymes are mainly due to differences in the rates of hydrolysis and not to differences in the affinities for the substrates.
Publication Date: 1976-05-13 PubMed ID: 5144DOI: 10.1016/0005-2744(76)90331-4Google Scholar: Lookup
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- Comparative Study
- Journal Article
Summary
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This research paper examines the enzyme kinetics of the pancreatic ribonucleases that come from cow, giraffe, horse, rat, and lesser rorqual with no significant differences found between the activities of these enzymes.
Understanding Enzyme Kinetics
- The paper delves into the concept of enzyme kinetics by examining the pancreatic ribonucleases from five mammalian species: cow, giraffe, horse, rat and lesser rorqual.
- Enzyme kinetics is a fundamental part of biochemistry that studies the rates at which enzymes catalyze reactions.
- In this case, the enzymes under study are pancreatic ribonucleases, a type of nuclease that cleaves RNA into smaller components.
- Three specific kinetic parameters are examined in this study: Km, k+2, and the ratio k+2/Km.
- Km (Michaelis-Menten constant) is a measure of the affinity of the enzyme for its substrate, k+2 is the rate at which the enzyme-substrate complex forms the product, and k+2/Km is a measure of the efficiency of the enzyme.
Substrates Used
- For the purpose of this study, the substrates used were 2′,3′-cyclic cytidine monophosphate and 2′,3′-cuclic uridine monophosphate.
- A substrate in the context of biochemistry is the molecule upon which an enzyme acts. In this case, these two compounds were the molecules broken down by the ribonucleases.
Findings of the Study
- Upon analysis, no significant differences were identified between the activities of the ribonucleases from the five different species.
- The relative differences that were noticed between the activities of the five enzymes were primarily due to differences in the rates of hydrolysis, not differences in the affinities for the substrates.
- Hydrolysis is the chemical breakdown of a compound due to reaction with water – in this context, it is the breakdown of the RNA components.
- This suggests that despite the species difference, the efficiency of these ribonucleases is relatively uniform across the board, emphasizing their fundamental role in biological processes.
Cite This Article
APA
Ronda GJ, Gaastra W, Beintema JJ.
(1976).
Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species.
Biochim Biophys Acta, 429(3), 853-859.
https://doi.org/10.1016/0005-2744(76)90331-4 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Artiodactyla
- Cattle
- Cytosine Nucleotides / metabolism
- Female
- Horses
- Hydrogen-Ion Concentration
- Kinetics
- Nucleotides, Cyclic / metabolism
- Pancreas / enzymology
- Rats
- Ribonucleases / metabolism
- Uracil Nucleotides / metabolism
- Whales
Citations
This article has been cited 3 times.- deMel VS, Doscher MS, Glinn MA, Martin PD, Ram ML, Edwards BF. Structural investigation of catalytically modified F120L and F120Y semisynthetic ribonucleases. Protein Sci 1994 Jan;3(1):39-50.
- Beintema JJ, Gaastra W, Lenstra JA, Welling GW, Fitch WM. The molecular evolution of pancreatic ribonuclease. J Mol Evol 1977 Sep 20;10(1):49-71.
- Beintema JJ, Gaastra W, Munniksma J. Primary structure of pronghorn pancreatic ribonuclease: close relationship between giraffe and pronghorn. J Mol Evol 1979 Nov;13(4):305-16.
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