1mok
From Proteopedia
(New page: 200px<br /><applet load="1mok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mok, resolution 2.80Å" /> '''NADPH DEPENDENT 2-KE...) |
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| - | [[Image:1mok.gif|left|200px]]<br /><applet load="1mok" size=" | + | [[Image:1mok.gif|left|200px]]<br /><applet load="1mok" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mok, resolution 2.80Å" /> | caption="1mok, resolution 2.80Å" /> | ||
'''NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE'''<br /> | '''NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is | + | The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is the terminal enzyme in a metabolic pathway that results in the conversion of propylene to the central metabolite acetoacetate in Xanthobacter autotrophicus Py2. This enzyme is an FAD-containing enzyme that is a member of the NADPH:disulfide oxidoreductase (DSOR) family of enzymes that include glutathione reductase, dihydrolipoamide dehydrogenase, trypanothione reductase, thioredoxin reductase, and mercuric reductase. In contrast to the prototypical reactions catalyzed by members of the DSOR family, the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M. The structure of 2-KPCC reveals a unique active site in comparison to those of other members of the DSOR family of enzymes and demonstrates how the enzyme architecture has been adapted for the more sophisticated biochemical reaction. In addition, comparison of the structures in the native state and in the presence of bound substrate indicates the binding of the substrate 2-ketopropyl-coenzyme M induces a conformational change resulting in the collapse of the substrate access channel. The encapsulation of the substrate in this manner is reminiscent of the conformational changes observed in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco). |
==About this Structure== | ==About this Structure== | ||
| - | 1MOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_sp. Xanthobacter sp.] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_sp. Xanthobacter sp.] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthobacter sp.]] | [[Category: Xanthobacter sp.]] | ||
| - | [[Category: Clark, D | + | [[Category: Clark, D D.]] |
| - | [[Category: Ensign, S | + | [[Category: Ensign, S A.]] |
| - | [[Category: Jang, S | + | [[Category: Jang, S B.]] |
| - | [[Category: Jeong, M | + | [[Category: Jeong, M S.]] |
[[Category: Nocek, B.]] | [[Category: Nocek, B.]] | ||
| - | [[Category: Peters, J | + | [[Category: Peters, J W.]] |
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: disulphide bond]] | [[Category: disulphide bond]] | ||
| Line 24: | Line 24: | ||
[[Category: nucleotide binding motifs]] | [[Category: nucleotide binding motifs]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:21 2008'' |
Revision as of 11:57, 21 February 2008
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NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE
Overview
The NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is the terminal enzyme in a metabolic pathway that results in the conversion of propylene to the central metabolite acetoacetate in Xanthobacter autotrophicus Py2. This enzyme is an FAD-containing enzyme that is a member of the NADPH:disulfide oxidoreductase (DSOR) family of enzymes that include glutathione reductase, dihydrolipoamide dehydrogenase, trypanothione reductase, thioredoxin reductase, and mercuric reductase. In contrast to the prototypical reactions catalyzed by members of the DSOR family, the NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M. The structure of 2-KPCC reveals a unique active site in comparison to those of other members of the DSOR family of enzymes and demonstrates how the enzyme architecture has been adapted for the more sophisticated biochemical reaction. In addition, comparison of the structures in the native state and in the presence of bound substrate indicates the binding of the substrate 2-ketopropyl-coenzyme M induces a conformational change resulting in the collapse of the substrate access channel. The encapsulation of the substrate in this manner is reminiscent of the conformational changes observed in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco).
About this Structure
1MOK is a Single protein structure of sequence from Xanthobacter sp. with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW, Biochemistry. 2002 Oct 29;41(43):12907-13. PMID:12390015
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