Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis.

View Full Paper

Ask AI

Bookmark

Population

Two probands deficient in lipoprotein lipase activity and available family members, along with in vitro COS…

Design

Preclinical

Authors

Discussion

May inform variant interpretation in LPL deficiency; confirms Asp156 essentiality but leaves open therapeutic translation.

Population

Two probands deficient in lipoprotein lipase (LPL) activity and available family members, along with in vitro COS cell models.

Intervention

Naturally occurring mutations in the LPL gene (Asp156Asn, Cys216Ser, and Asp156Gly) and in vitro site-directed mutagenesis.

Outcome

LPL catalytic activity and structure/function relationships.surrogate

Naturally occurring mutations at Asp156 demonstrate that this residue is essential for the catalytic activity of human lipoprotein lipase.

H et al. (1992) studied this question.

View Full Paper

Ask AI

Bookmark