1chm
From Proteopedia
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| - | [[Image:1chm.gif|left|200px]] | + | [[Image:1chm.gif|left|200px]] |
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| - | '''ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES''' | + | {{Structure |
| + | |PDB= 1chm |SIZE=350|CAPTION= <scene name='initialview01'>1chm</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CHM is a [ | + | 1CHM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1696320 1696320] |
[[Category: Creatinase]] | [[Category: Creatinase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: creatinase]] | [[Category: creatinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:31 2008'' |
Revision as of 08:24, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Activity: | Creatinase, with EC number 3.5.3.3 | ||||||
| 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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