May 1, 1996Biochemical JournalOpen Access

Rat endothelin-converting enzyme-1 forms a dimer through Cys412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11

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Population

Rat endothelin-converting enzyme-1 (ECE-1) and its mutants

Comparison

Site-directed mutagenesis vs Wild-type ECE-1 and neutral endopeptidase-24.11

Design

Preclinical

Authors

Discussion

Cys412-dependent dimerization optimizes rat ECE-1 kinetics; leaves open its role in human endothelin regulation or cardiovascular therapeutics.

Population

Rat endothelin-converting enzyme-1 (ECE-1) and its mutants

Intervention

Site-directed mutagenesis (C412S, E592Q, E651Q, H716Q, Arg129, Glu752 substitutions)

Comparator

Wild-type ECE-1 and neutral endopeptidase-24.11 (NEP)

Outcome

Enzyme dimerization, catalytic activity (Km, kcat), and substrate bindingsurrogate

Dimerization of rat ECE-1 via Cys412 is crucial for its optimal catalytic efficiency in converting big endothelins to endothelins.

Shimada et al. (1996) studied this question.

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Cys412-dependent dimerization optimizes rat ECE-1 kinetics; leaves open its role in human endothelin regulation or cardiovascular therapeutics.