A Biologic Institute challenge to Darwinism: two protein chains, combined length over 1,400 amino acid residues
|May 1, 2012||Posted by News under Cell biology, Intelligent Design, News|
In “Intricate Co-ordination”(Biologic Perspectives,, April 30, 3012), Biologic Institute senior scientist Ann Gauger explains,
Meet carbamoyl phosphate synthetase (CPS), a remarkably complex enzyme. This enzyme uses bicarbonate, glutamine, ATP, and water to make carbamoyl phosphate via a multi-step reaction at three separate active sites, involving several unstable intermediates. [details linked]
CPS is made of two protein chains with a combined length of over 1,400 amino acid residues. We now know from extensive biochemical data that a fully coupled CPS requires the hydrolysis of one glutamine and two molecules of MgATP for every molecule of carbamoyl phosphate formed. …
How does a neo-Darwinian process evolve an enzyme like this? Even if enzymes that carried out the various partial reactions could have evolved separately, the coordination and combining of those domains into one huge enzyme is a feat of engineering beyond anything we can do. More.
Note: Biologic Institute is not to be confused with Biologos. The former is a research group that agrees that there is design in nature, and publishes journal papers on relevant issues. The latter was founded by NIH head Francis Collins to help theologians and scientists promote Darwinism to Christians.