Phenylglyoxal modification of cardiac myosin S-1. Evidence for essential arginine residues at the active site
The role of arginine residues in the catalytic activity of cardiac myosin subfragment-1 (S-1) was investigated by selective modification with phenylglyoxal. Incorporation of about 2.8 mol of phenylglyoxal/mol of S-1 decreased Ca2+-ATPase activity about 50%. Gelation of the protein occurred at about 70% inactivation; however, extrapolation to complete inactivation indicated that loss of activity correlated with modification of about 4 arginyls/mol. Partial inactivation of S-1 with phenylglyoxal also decreased MgADP binding markedly. When S-1 was modified in the presence of 5 mM MgADP, only 2 arginyls/mol were blocked and there was almost complete protection against loss of Ca2+-ATPase activity and ability to bind MgADP. Similar protection against inactivation by phenylglyoxal was obtained with MgATP or sodium pyrophosphate, but not with MgAMP or magnesium adenosine. These results suggest that 2 arginyls/myosin head are important for enzymatic activity, possibly serving as attachment points between enzyme and substrate. These essential arginyls were localized to a 17,000-dalton cyanogen bromide peptide from the heavy chain fragment of S-1.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1979 |
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| Erschienen: |
1979 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:254 |
|---|---|
| Enthalten in: |
The Journal of biological chemistry - 254(1979), 24 vom: 25. Dez., Seite 12647-52 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Morkin, E [VerfasserIn] |
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| Anmerkungen: |
Date Completed 28.01.1980 Date Revised 10.02.2021 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM001595865 |
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| 100 | 1 | |a Morkin, E |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Phenylglyoxal modification of cardiac myosin S-1. Evidence for essential arginine residues at the active site |
| 264 | 1 | |c 1979 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 28.01.1980 | ||
| 500 | |a Date Revised 10.02.2021 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a The role of arginine residues in the catalytic activity of cardiac myosin subfragment-1 (S-1) was investigated by selective modification with phenylglyoxal. Incorporation of about 2.8 mol of phenylglyoxal/mol of S-1 decreased Ca2+-ATPase activity about 50%. Gelation of the protein occurred at about 70% inactivation; however, extrapolation to complete inactivation indicated that loss of activity correlated with modification of about 4 arginyls/mol. Partial inactivation of S-1 with phenylglyoxal also decreased MgADP binding markedly. When S-1 was modified in the presence of 5 mM MgADP, only 2 arginyls/mol were blocked and there was almost complete protection against loss of Ca2+-ATPase activity and ability to bind MgADP. Similar protection against inactivation by phenylglyoxal was obtained with MgATP or sodium pyrophosphate, but not with MgAMP or magnesium adenosine. These results suggest that 2 arginyls/myosin head are important for enzymatic activity, possibly serving as attachment points between enzyme and substrate. These essential arginyls were localized to a 17,000-dalton cyanogen bromide peptide from the heavy chain fragment of S-1 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 4 | |a Research Support, U.S. Gov't, P.H.S. | |
| 650 | 7 | |a Aldehydes |2 NLM | |
| 650 | 7 | |a Arginine |2 NLM | |
| 650 | 7 | |a 94ZLA3W45F |2 NLM | |
| 650 | 7 | |a Myosins |2 NLM | |
| 650 | 7 | |a EC 3.6.4.1 |2 NLM | |
| 650 | 7 | |a Calcium-Transporting ATPases |2 NLM | |
| 650 | 7 | |a EC 7.2.2.10 |2 NLM | |
| 650 | 7 | |a Phenylglyoxal |2 NLM | |
| 650 | 7 | |a N45G3015PA |2 NLM | |
| 700 | 1 | |a Flink, I L |e verfasserin |4 aut | |
| 700 | 1 | |a Banerjee, S K |e verfasserin |4 aut | |
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