1h2g
From Proteopedia
(New page: 200px<br /> <applet load="1h2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h2g, resolution 2.00Å" /> '''ALTERED SUBSTRATE S...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H2G is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CA and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2G OCA]]. | + | 1H2G is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CA and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11]]. Structure known Active Site: CA1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2G OCA]]. |
==Reference== | ==Reference== | ||
Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding., Morillas M, McVey CE, Brannigan JA, Ladurner AG, Forney LJ, Virden R, Biochem J. 2003 Apr 1;371(Pt 1):143-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12511194 12511194] | Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding., Morillas M, McVey CE, Brannigan JA, Ladurner AG, Forney LJ, Virden R, Biochem J. 2003 Apr 1;371(Pt 1):143-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12511194 12511194] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Penicillin amidase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Brannigan, J.A.]] | [[Category: Brannigan, J.A.]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''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 12:24:24 2007'' |
Revision as of 10:19, 30 October 2007
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ALTERED SUBSTRATE SPECIFICITY MUTANT OF PENICILLIN ACYLASE
Overview
Two mutant forms of penicillin acylase from Escherichia coli strains, selected using directed evolution for the ability to use, glutaryl-L-leucine for growth [Forney, Wong and Ferber (1989) Appl., Environ. Microbiol. 55, 2550-2555], are changed within one codon, replacing the B-chain residue Phe(B71) with either Cys or Leu. Increases, of up to a factor of ten in k (cat)/ K (m) values for substrates, possessing a phenylacetyl leaving group are consistent with a decrease in, K (s). Values of k (cat)/ K (m) for glutaryl-L-leucine are increased at, least 100-fold. A decrease in k (cat)/ K (m) for the Cys(B71) mutant with, increased pH is consistent with binding of the uncharged glutaryl group., The mutant proteins are more resistant to urea denaturation monitored by, protein fluorescence, to ... [(full description)]
About this Structure
1H2G is a [Protein complex] structure of sequences from [Escherichia coli] with CA and EDO as [ligands]. Active as [Penicillin amidase], with EC number [3.5.1.11]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].
Reference
Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding., Morillas M, McVey CE, Brannigan JA, Ladurner AG, Forney LJ, Virden R, Biochem J. 2003 Apr 1;371(Pt 1):143-50. PMID:12511194
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