1gkj
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1GKJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with SO4 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1GKJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with SO4 and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Histidine_ammonia-lyase Histidine ammonia-lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.3 4.3.1.3]]. Structure known Active Site: MIO. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GKJ OCA]]. |
==Reference== | ==Reference== | ||
Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism., Baedeker M, Schulz GE, Eur J Biochem. 2002 Mar;269(6):1790-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11895450 11895450] | Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism., Baedeker M, Schulz GE, Eur J Biochem. 2002 Mar;269(6):1790-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11895450 11895450] | ||
| + | [[Category: Histidine ammonia-lyase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:23:58 2007'' |
Revision as of 08:19, 30 October 2007
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HISTIDINE AMMONIA-LYASE (HAL) MUTANT Y280F FROM PSEUDOMONAS PUTIDA
Overview
Histidine ammonia-lyase (EC 4.3.1.3) catalyzes the nonoxidative, elimination of the alpha-amino group of histidine using a, 4-methylidene-imidazole-5-one (MIO), which is formed autocatalytically, from the internal peptide segment 142Ala-Ser-Gly. The structure of the, enzyme inhibited by a reaction with l-cysteine was established at the very, high resolution of 1.0 A. Five active center mutants were produced and, their catalytic activities were measured. Among them, mutant Tyr280-->Phe, could be crystallized and its structure could be determined at 1.7 A, resolution. It contains a planar sp2-hybridized 144-N atom of MIO, in, contrast to the pyramidal sp3-hybridized 144-N of the wild-type. With the, planar 144-N atom, MIO assumes the conformation of a putative intermediate, aromatic ... [(full description)]
About this Structure
1GKJ is a [Single protein] structure of sequence from [Pseudomonas putida] with SO4 and GOL as [ligands]. Active as [Histidine ammonia-lyase], with EC number [4.3.1.3]. Structure known Active Site: MIO. Full crystallographic information is available from [OCA].
Reference
Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism., Baedeker M, Schulz GE, Eur J Biochem. 2002 Mar;269(6):1790-7. PMID:11895450
Page seeded by OCA on Tue Oct 30 10:23:58 2007
