1chm
From Proteopedia
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|PDB= 1chm |SIZE=350|CAPTION= <scene name='initialview01'>1chm</scene>, resolution 1.9Å | |PDB= 1chm |SIZE=350|CAPTION= <scene name='initialview01'>1chm</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CMS:CARBAMOYL SARCOSINE'>CMS</scene> | + | |LIGAND= <scene name='pdbligand=CMS:CARBAMOYL+SARCOSINE'>CMS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Creatinase Creatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.3 3.5.3.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatinase Creatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.3 3.5.3.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1chm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chm OCA], [http://www.ebi.ac.uk/pdbsum/1chm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1chm RCSB]</span> | ||
}} | }} | ||
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[[Category: Moellering, H.]] | [[Category: Moellering, H.]] | ||
[[Category: Schumacher, G.]] | [[Category: Schumacher, G.]] | ||
| - | [[Category: CMS]] | ||
[[Category: creatinase]] | [[Category: creatinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:21:49 2008'' |
Revision as of 16:21, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Activity: | Creatinase, with EC number 3.5.3.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES
Overview
Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N(3) atom of the guanidinium group. OH- 377 adds to the C(1) atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site.
About this Structure
1CHM is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures., Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Russmann L, Schumacher G, J Mol Biol. 1990 Jul 20;214(2):597-610. PMID:1696320
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