1vsb: Difference between revisions
New page: left|200px<br /> <applet load="1vsb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vsb, resolution 2.1Å" /> '''SUBTILISIN CARLSBERG... |
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==About this Structure== | ==About this Structure== | ||
1VSB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VSB OCA]]. | 1VSB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]]. Active as [[http://en.wikipedia.org/wiki/Subtilisin Subtilisin]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]]. Structure known Active Sites: ACT, M1 and M2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VSB OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Subtilisin]] | |||
[[Category: Eger, B.T.]] | [[Category: Eger, B.T.]] | ||
[[Category: Hynes, R.C.]] | [[Category: Hynes, R.C.]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:14:22 2007'' | ||
Revision as of 15:09, 30 October 2007
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SUBTILISIN CARLSBERG L-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
OverviewOverview
In order to probe the structural basis of stereoselectivity in the serine, protease family, a series of enantiomeric boronic acids, RCH2CH(NHCOCH3)B(OH)2 has been synthesized and kinetically characterized, as transition-state analog inhibitors using alpha-chymotrypsin and, subtilisin Carlsberg as model systems. When the R-substituent in this, series was changed from a p-chlorophenyl to a 1-naphthyl group, alpha-chymotrypsin, but not subtilisin, reversed its usual preference for, l-enantiomers and bound more tightly to the D-enantiomer [Martichonok, V., & Jones, J. B. (1996) J. Am. Chem. Soc. 118, 950-958]. The structural, factors responsible for the differences in stereoselectivity between the, two enzymes have been explored by X-ray crystallographic examination of, subtilisin ... [(full description)]
About this StructureAbout this Structure
1VSB is a [Single protein] structure of sequence from [Bacillus licheniformis]. Active as [Subtilisin], with EC number [3.4.21.62]. Structure known Active Sites: ACT, M1 and M2. Full crystallographic information is available from [OCA].
ReferenceReference
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:9425066
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