2cel: Difference between revisions
New page: left|200px<br /> <applet load="2cel" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cel, resolution 2.0Å" /> '''ACTIVE-SITE MUTANT E... |
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==About this Structure== | ==About this Structure== | ||
2CEL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | 2CEL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]] with NAG and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91]]. Structure known Active Sites: CAA, CAB, CTA and CTB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CEL OCA]]. | ||
==Reference== | ==Reference== | ||
Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei., Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA, J Mol Biol. 1996 Nov 29;264(2):337-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8951380 8951380] | Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei., Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA, J Mol Biol. 1996 Nov 29;264(2):337-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8951380 8951380] | ||
[[Category: Cellulose 1,4-beta-cellobiosidase]] | |||
[[Category: Hypocrea jecorina]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Divne, C.]] | [[Category: Divne, C.]] | ||
[[Category: Jones, T.A.]] | [[Category: Jones, T.A.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''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 13:39:20 2007'' | ||
Revision as of 14:34, 30 October 2007
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ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE
OverviewOverview
The roles of the residues in the catalytic trio Glu212-Asp214-Glu217 in, cellobiohydrolase I (CBHI) from Trichoderma reesei have been investigated, by changing these residues to their isosteric amide counterparts. Three, mutants, E212Q, D214N and E217Q, were constructed and expressed in T., reesei. All three point mutations significantly impair the catalytic, activity of the enzyme, although all retain some residual activity. On the, small chromophoric substrate CNP-Lac, the kcat values were reduced to, 1/2000, 1/85 and 1/370 of the wild-type activity, respectively, whereas, the KM values remained essentially unchanged. On insoluble crystalline, cellulose, BMCC, no significant activity was detected for the E212Q and, E217Q mutants, whereas the D214N mutant retained residual activity. The, ... [(full description)]
About this StructureAbout this Structure
2CEL is a [Single protein] structure of sequence from [Hypocrea jecorina] with NAG and CA as [ligands]. Active as [Cellulose 1,4-beta-cellobiosidase], with EC number [3.2.1.91]. Structure known Active Sites: CAA, CAB, CTA and CTB. Full crystallographic information is available from [OCA].
ReferenceReference
Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei., Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA, J Mol Biol. 1996 Nov 29;264(2):337-49. PMID:8951380
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