Jianying Shi

TL;DR: Major advances in the development of new strains and vectors, improved techniques, and the commercial availability of these tools coupled with a better understanding of the biology of Pichia species have led to this microbe’s value and power in commercial and research labs alike.

TL;DR: It is demonstrated that glutamic acid 3 and histidine 5 are necessary for malonyl-CoA binding and inhibition of L-CPTI by malonygCoA but are not required for catalysis.

TL;DR: Results demonstrate that the N-terminal residues critical for activity and malonyl CoA sensitivity in M-CPTI are different from those of L- CPTI, suggesting that the amino acid residues responsible for the differing sensitivity to malonyL CoA are not located in this N-Terminal region.

TL;DR: The functional expression of the human heart/skeletal muscle isoform of CPT-I (M-CPT-I) in the yeast Pichia pastoris is reported, which is the first report of the expression of a heart C PT-I in a system devoid of endogenous CPT activity and the functional characterization of a human heart M-CPTs in the absence of the liver isoform andCPT-II.

TL;DR: This is the first report to demonstrate a critical role for these perfectly conserved first 18 N-terminal amino acid residues of L-CPTI in malonyl-CoA sensitivity and binding.