1j0a
From Proteopedia
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|PDB= 1j0a |SIZE=350|CAPTION= <scene name='initialview01'>1j0a</scene>, resolution 2.5Å | |PDB= 1j0a |SIZE=350|CAPTION= <scene name='initialview01'>1j0a</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5 | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_deaminase 1-aminocyclopropane-1-carboxylate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.7 3.5.99.7] | |ACTIVITY= [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_deaminase 1-aminocyclopropane-1-carboxylate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.7 3.5.99.7] | ||
|GENE= | |GENE= | ||
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[[Category: plp dependent]] | [[Category: plp dependent]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:17:05 2008'' |
Revision as of 10:17, 23 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | 1-aminocyclopropane-1-carboxylate deaminase, with EC number 3.5.99.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of the ACC deaminase homologue
Overview
1-Aminocyclopropane-l-carboxylate deaminase (ACCD) is a pyridoxal 5/-phosphate dependent enzyme that shows deaminase activity toward ACC, a precursor of plant hormone ethylene. ACCD from some soil bacteria has been reported to be able to break the cyclopropane ring of ACC to yield a-ketobutyrate and ammonia. We reported the crystal structure of ACCD from the yeast Hansenula saturnus in the absence/presence of substrate ACC, and proposed its ingenious reaction mechanisms. In order to study the enzyme further, we overexpressed the ACCD homologue protein (phAHP) from the fully decoded hyperthermophilic archearon, Pyrococcus horikoshii OT3. However, phAHP does not show ACCD activity at high temperature as well as at room temperature, though it has significant sequence similarity. Instead of ACCD activity, the GC-MS analysis and enzymatic method show that phAHP has deaminase activity toward L and D-serine. Here, we present the crystal structures of the native and ACC-complexed phAHP. The overall topology of the phAHP structure is very similar to that of ACCD; however, critical differences were observed around the active site. Here, the differences of enzymatic activity between phAHP and ACCD are discussed based on the structural differences of these two proteins. We suggest that the catalytic disagreement between these two enzymes comes from the difference of the residues near the pyridine ring of pyridoxal 5'-phosphate (PLP), not the difference of the catalytic residues themselves. We also propose a condition necessary in the primary sequence to have ACCD activity.
About this Structure
1J0A is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
Reference
Structural and enzymatic properties of 1-aminocyclopropane-1-carboxylate deaminase homologue from Pyrococcus horikoshii., Fujino A, Ose T, Yao M, Tokiwano T, Honma M, Watanabe N, Tanaka I, J Mol Biol. 2004 Aug 20;341(4):999-1013. PMID:15328614
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