Key result
Mutation of Trp-512 to phenylalanine in smooth muscle heavy meromyosin reduced the MgATP-induced fluorescence emission increase to 5%, compared to 25-27% in wild-type, identifying 512 as the sensitive Trp.
Population
Smooth muscle heavy meromyosin (HMM) preparations (wild-type, sham-mutated, W441F HMM, W512F HMM)
Comparison
Mutation of specific tryptophan residues and… vs Wild-type and sham-mutated HMM
Design
Preclinical
Authors
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Trp-512 identified as MgATP-sensitive residue in smooth muscle myosin; extends structural insights but leaves functional and clinical relevance open.
Absolute Event Rate: 5% vs 25%
Trp-512 is identified as the sensitive tryptophan residue in smooth muscle myosin that responds to nucleotide binding, with its mutation causing significant functional alterations.
Onishi et al. (2000) studied this question. W512F mutation in smooth muscle heavy meromyosin vs. Wild-type and W441F HMMs was evaluated on Fluorescence emission increase upon adding MgATP. Mutation of Trp-512 to phenylalanine in smooth muscle heavy meromyosin reduced the MgATP-induced fluorescence emission increase to 5%, compared to 25-27% in wild-type, identifying 512 as the sensitive Trp.
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