Abstract：
:Synthetic peptides corresponding to the phosphorylation site in the myosin regulatory light chain from smooth muscle, Lys-Lys-Arg-Ala-Arg-Ala-Thr-Ser-Asn-Val-Phe-Ala ([Ala14,15]MLC(11-23] and containing a variety of hydroxyamino acid analogs at position 19, were tested as substrates for the smooth muscle myosin light chain kinase. Peptide analogs containing either D-serine or cis-hydroxyproline were not phosphorylated. The corresponding trans-hydroxyproline containing peptide was poorly phosphorylated with a Km of 2.3 microM and a Vmax of 3 X 10(-3) mumol.min-1.mg-1 compared to a Km of 12.5 microM and a Vmax of 1.43 mumol.min-1.mg-1 for the parent peptide. All three hydroxyamino acid analog peptides acted as relatively potent inhibitors of myosin light chain phosphorylation with Ki values in the range 7.5-10 microM, comparable to 7 microM for the parent peptide. Thus the failure of the hydroxyamino acid analog peptides to act as effective substrates was not the result of poor binding to the enzyme. In contrast, the same substitutions made in the peptide substrate for the cAMP-dependent protein kinase resulted in poor inhibitors. It is likely that the hydroxyl group of the substituting amino acids in the myosin light chain peptide analogs is not presented in the correct orientation in the active site for transfer of the phosphate group.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Pearson RB,Floyd DM,Hunt JT,Lee VG,Kemp BEdoi
10.1016/0003-9861(88)90421-3subject
Has Abstractpub_date
1988-01-01 00:00:00pages
37-44issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(88)90421-3journal_volume
260pub_type
杂志文章abstract：:The kinetic analysis of the enzymatic reaction catalyzed by glycogen phosphorylase b from the rabbit skeletal muscle has been carried out in the direction of glycogen synthesis under the conditions of the saturation of the enzyme by glycogen. The applicability of 12 different variants of the Monod-Wyman-Changeux model...
journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章,评审
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journal_title：Archives of biochemistry and biophysics
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pub_type： 杂志文章
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章,评审
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更新日期：2012-07-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章,评审
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journal_title：Archives of biochemistry and biophysics
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更新日期：2007-01-15 00:00:00
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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更新日期：2000-07-15 00:00:00
abstract：:A cDNA from Arabidopsis thaliana resembling S-formylglutathione hydrolase (SFGH), an enzyme with putative roles in formaldehyde detoxification in animals and microorganisms, has been cloned and expressed in Escherichia coli. The purified recombinant Arabidopsis enzyme (AtSFGH) was a dimer composed of 31-kDa subunits. ...
journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1006/abbi.2002.2772
更新日期：2002-03-15 00:00:00
