Abstract:
:Glutamine synthetase from a Gram-positive acid-fast bacterium, Mycobacterium smegmatis, was purified to homogeneity from cells grown with glycerol-bouillon medium. Electron micrographs of the enzyme revealed a dodecameric arrangement of its subunits in two superimposed hexagonal rings, similar to the structure of glutamine synthetase of Escherichia coli. Disc electrophoresis in the presence of sodium dodecyl sulfate indicated a subunit molecular weight of 56,000. The sedimentation coefficient of the native enzyme was estimated to be 19.4S by ultracentrifugation in a sucrose gradient. Like the E. coli enzyme, the glutamine synthetase from M. smegmatis is regulated by adenylylation/deadenylylation. This conclusion was based on studies of the effect of snake venom phosphodiesterase treatment on the catalytic and spectral properties of the isolated enzyme. The AMP released from the enzyme by the phosphodiesterase was identified by thin-layer chromatography. Despite the structural similarity of both enzymes, striking differences were found between the catalytic properties of M. smegmatis and E. coli glutamine synthetases. The divalent cation specificity of the M. smegmatis enzyme was not altered by adenylylation of the enzyme, and deadenylylation of the enzyme caused a significant increase in the specific activities for both biosynthetic and transfer reactions with either Mg2+ or Mn2+.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Kimura K,Yagi K,Matsuoka Kdoi
10.1093/oxfordjournals.jbchem.a134768subject
Has Abstractpub_date
1984-06-01 00:00:00pages
1559-67issue
6eissn
0021-924Xissn
1756-2651journal_volume
95pub_type
杂志文章abstract::Human serum sulfotransferase activities were measured in normal controls and patients with macular corneal dystrophy (MCD), an inherited disorder characterized by the decreased sulfation of keratan sulfate in the corneal stroma and serum, using two kinds of acceptor: partially desulfated keratan sulfate and a trisacch...
journal_title:Journal of biochemistry
pub_type: 杂志文章
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journal_title:Journal of biochemistry
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a133945
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a130800
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journal_title:Journal of biochemistry
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pub_type: 杂志文章
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1984-02-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a121985
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pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:1984-06-01 00:00:00
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journal_title:Journal of biochemistry
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更新日期:1991-09-01 00:00:00
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更新日期:2006-05-01 00:00:00