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Direct photoaffinity labeling of gizzard myosin with [3H]uridine diphosphate places Glu185 of the heavy chain at the active site

Autor: T E, Garabedian, R G, Yount

Publikováno v: The Journal of biological chemistry. 265(36)

The active site of chicken gizzard myosin was labeled by direct photoaffinity labeling with [3H]UDP. [3H] UDP was stably trapped at the active site by addition of vanadate (Vi) and Co2+. The extraordinary stability of the myosin.Co2+.[3H]UDP.Vi compl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aa20fc9574a7d13890d772e059e8e2dc
https://pubmed.ncbi.nlm.nih.gov/1979981

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Photolabeling of the 6 and 10 S conformations of gizzard myosin with 3'(2')-O-(4-Benzoyl)benzoyl-ATP. Proline 324 is near the active site

Autor: D G, Cole, R G, Yount

Publikováno v: The Journal of biological chemistry. 265(36)

3'(2')-O-(4-Benzoyl)benzoyl-ATP (Bz2ATP) was used as a photoaffinity label of the ATP binding site of unphosphorylated chicken gizzard myosin. Specific photolabeling of the active site of 6 S myosin was assured by forming a stable myosin.Co(II)Bz2ADP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ad037c399bec0b5ada6e50df953be9c6
https://pubmed.ncbi.nlm.nih.gov/2266144

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Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. II. Stoichiometry and subunit location of labeling

Autor: R G Yount, L E Greene

Publikováno v: Journal of Biological Chemistry. 252:1681-1688

The reaction of bovine cardiac myosin with the site-specific purine disulfide analog of ATP, 6,6'-dithiobis (inosinyl imidodiphosphate), was studied to determine the stoichiometry of labeling and subunit location of the reactive cysteines. The analog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4e6ea3624a973b17d6702ca71b99ad89
https://doi.org/10.1016/s0021-9258(17)40602-8

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Photochemical probes of the active site of myosin. Irradiation of trapped 3'-O-(4-benzoyl)benzoyladenosine 5'-triphosphate labels the 50-kilodalton heavy chain tryptic peptide

Autor: R G Yount, R Mahmood

Publikováno v: Journal of Biological Chemistry. 259:12956-12959

3'-O-(4-Benzoyl)benzoyl-ATP (Bz2ATP), an analog of ATP containing a photoreactive benzophenone moiety, was used as a probe of the ATP binding site of myosin subfragment 1 (SF1). The inactivation of SF1 NH+4-EDTA ATPase by the bifunctional thiol cross

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::16254f3f4ab41da46f690818f3dd5ec6
https://doi.org/10.1016/s0021-9258(18)90639-3

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Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. I. Kinetics of inactivation and binding of adenylyl imidodiphosphate

Autor: R G Yount, L E Greene

Publikováno v: Journal of Biological Chemistry. 252:1673-1680

Bovine cardiac myosin ATPase activity was rapidly inactivated by the purine disulfide analog of ATP,6,6'-dithiobis(inosinyl imidodiphosphate). Kinetic investigations showed that this analog acted as a site-specific reagent at 0 degrees with a Ki of 1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1b45631403971b512704f4c790af03ed
https://doi.org/10.1016/s0021-9258(17)40601-6

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ATP analogs

Autor: R G, Yount

Publikováno v: Advances in enzymology and related areas of molecular biology. 43

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::024d7f84fff11dd7e8d9c510137a2381
https://pubmed.ncbi.nlm.nih.gov/890

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Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. II. Stoichiometry and subunit location of labeling

Autor: L E, Greene, R G, Yount

Publikováno v: The Journal of biological chemistry. 252(5)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5af04cff59c7d84d7d7def409a59f42b
https://pubmed.ncbi.nlm.nih.gov/138684

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