Document Detail


Autophosphorylation of skeletal muscle myosin light chain kinase.
MedLine Citation:
PMID:  1627555     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ca2+/calmodulin-dependent myosin light chain kinase phosphorylates the regulatory light chain of myosin. Rabbit skeletal muscle myosin light chain kinase also catalyzes a Ca2+/calmodulin-dependent autophosphorylation with a rapid rate of incorporation of 1 mol of 32P/mol of kinase and a slower rate of incorporation up to 1.52 mol of 32P/mol. Autophosphorylation was inhibited by a peptide substrate that has a low Km value for myosin light chain kinase. Autophosphorylation at both rates was concentration-independent, indicating an intramolecular mechanism. There were no significant changes in catalytic properties toward light chain and MgATP substrates or in calmodulin activation properties upon autophosphorylation. After digestion with V8 protease, phosphopeptides were purified and sequenced. Two phosphorylation sites were identified, Ser 160 and Ser 234, with the former associated with the rapid rate of phosphorylation. Both sites are located amino terminal of the catalytic domain. These results indicate that the extended "tail" region of the enzyme can fold into the active site of the kinase.
Authors:
Z H Gao; C R Moomaw; J Hsu; C A Slaughter; J T Stull
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  31     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1992 Jul 
Date Detail:
Created Date:  1992-08-18     Completed Date:  1992-08-18     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  6126-33     Citation Subset:  IM    
Affiliation:
Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Amino Acid Sequence
Animals
Calcium / pharmacology
Calmodulin / pharmacology
Cyanogen Bromide
Egtazic Acid / pharmacology
Electrophoresis, Polyacrylamide Gel
Kinetics
Molecular Sequence Data
Muscles / enzymology*
Myosin-Light-Chain Kinase / chemistry,  metabolism*
Peptide Fragments / chemistry,  isolation & purification,  metabolism
Peptide Mapping
Phosphorus Radioisotopes
Phosphorylation
Rabbits
Serine Endopeptidases / metabolism
Grant Support
ID/Acronym/Agency:
HL06296/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Calmodulin; 0/Peptide Fragments; 0/Phosphorus Radioisotopes; 506-68-3/Cyanogen Bromide; 56-65-5/Adenosine Triphosphate; 67-42-5/Egtazic Acid; 7440-70-2/Calcium; EC 2.7.11.18/Myosin-Light-Chain Kinase; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.19/glutamyl endopeptidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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