dc.contributor.author |
Leshchinskaya I. |
|
dc.contributor.author |
Shakirov E. |
|
dc.contributor.author |
Itskovitch E. |
|
dc.contributor.author |
Balaban N. |
|
dc.contributor.author |
Mardanova A. |
|
dc.contributor.author |
Sharipova M. |
|
dc.contributor.author |
Blagova E. |
|
dc.contributor.author |
Levdikov V. |
|
dc.contributor.author |
Kuranova I. |
|
dc.contributor.author |
Rudenskaya G. |
|
dc.contributor.author |
Stepanov V. |
|
dc.date.accessioned |
2018-09-17T20:08:41Z |
|
dc.date.available |
2018-09-17T20:08:41Z |
|
dc.date.issued |
1997 |
|
dc.identifier.issn |
0006-2979 |
|
dc.identifier.uri |
https://dspace.kpfu.ru/xmlui/handle/net/133094 |
|
dc.description.abstract |
A homogeneous glutamyl endopeptidase splitting peptide bonds of glutamic and, rarely, of aspartic acid residues in peptides and proteins was isolated from Bacillus intermedius 3-19 culture filtrate using chromatography on CM-cellulose and Mono S. The enzyme molecular mass is 29 kD and the p/ is 8.4. The proteinase is inhibited by DFP. The enzyme, like other glutamyl endopeptidases, reveals two pH optima (pH 7.5 and 9.0) for casein and one (pH 8.0) for Z-Glu-pNA hydrolysis. The Km for the hydrolysis of the latter substrate is 6 mM. The enzyme activity is optimal at 55°C. The enzyme is stable in the pH range 6.5-11.0. Its N-terminal sequence shows 56% coinciding residues when compared with that of Bacillus licheniformis glutamyl endopeptidase. Crystal prisms or plates 0.25-0.3 × 0.15 × 0.07-0.1 mm have been grown using the vapor diffusion technique in a hanging drop followed by macroseeding. The crystals belong to the space group B2 with the following unit cell parameters: a = 69.59 Å; b = 61.61 Å; c = 56.11 Å; γ = 117.57°. The X-ray data set to 1.7 Å resolution has been collected on an automatic synchrotron (EMBL Hamburg Station). |
|
dc.relation.ispartofseries |
Biochemistry (Moscow) |
|
dc.subject |
Crystallization |
|
dc.subject |
Glutamyl endopeptidase (Bacillus intermedius) |
|
dc.subject |
Isolation |
|
dc.subject |
Proteases |
|
dc.subject |
Specificity |
|
dc.title |
Glutamyl endopeptidase of Bacillus intermedius strain 3-19. Purification, properties, and crystallization |
|
dc.type |
Article |
|
dc.relation.ispartofseries-issue |
8 |
|
dc.relation.ispartofseries-volume |
62 |
|
dc.collection |
Публикации сотрудников КФУ |
|
dc.relation.startpage |
903 |
|
dc.source.id |
SCOPUS00062979-1997-62-8-SID0031196092 |
|