Related Experiment Video
Updated: Apr 30, 2026

Primary Endodermal Epithelial Cell Culture from the Yolk Sac Membrane of Japanese Quail Embryos
Published on: March 10, 2016
Biochemistry: role of PQQ as a mammalian enzyme cofactor?
Leigh M Felton1, Chris Anthony
1School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK.
Abstract:
The announcement by Kasahara and Kato of a new redox-cofactor vitamin for mammals, pyrroloquinoline quinone (PQQ), was based on their claim that an enzyme, predicted to be involved in mouse lysine metabolism, is a PQQ-dependent dehydrogenase. However, this claim was dependent on a sequence analysis using databases that inappropriately label beta-propeller sequences as PQQ-binding motifs. What the evidence actually suggests is that the enzyme is an interesting novel protein that has a seven-bladed beta-propeller structure, but there is nothing to indicate that it is a PQQ-dependent dehydrogenase.
More Related Videos
11:56Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
07:20Author Spotlight: Integrating Traditional Chinese Medicine with Modern Pharmacology and Genomics for Assessing Postmenopausal Osteoporosis in Mice
Published on: August 23, 2024
Related Concept Videos
Bacterial Signaling
Protein Digestion
Hormonal Regulation
Cofactors and Coenzymes
Cofactors and Coenzymes
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Gene Regulation in Microbial Communities: Quorum Sensing