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2a89
From Proteopedia
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[[Image:2a89.gif|left|200px]] | [[Image:2a89.gif|left|200px]] | ||
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'''Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme''' | '''Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme''' | ||
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[[Category: Mathews, F S.]] | [[Category: Mathews, F S.]] | ||
[[Category: Zhao, G.]] | [[Category: Zhao, G.]] | ||
| - | [[Category: | + | [[Category: Flavoprotein]] |
| - | [[Category: | + | [[Category: Oxidase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:44:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:44, 3 May 2008
Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme
Overview
Monomeric sarcosine oxidase (MSOX) is a flavoprotein that contains covalently bound FAD [8a-(S-cysteinyl)FAD] and catalyzes the oxidation of sarcosine (N-methylglycine) and other secondary amino acids, such as l-proline. Our previous studies showed that N-(cyclopropyl)glycine (CPG) acts as a mechanism-based inactivator of MSOX [Zhao, G., et al. (2000) Biochemistry 39, 14341-14347]. The reaction results in the formation of a modified reduced flavin that can be further reduced and stabilized by treatment with sodium borohydride. The borohydride-reduced CPG-modified enzyme exhibits a mass increase of 63 +/- 2 Da as compared with native MSOX. The crystal structure of the modified enzyme, solved at 1.85 A resolution, shows that FAD is the only site of modification. The modified FAD contains a fused five-membered ring, linking the C(4a) and N(5) atoms of the flavin ring, with an additional oxygen atom bound to the carbon atom attached to N(5) and a tetrahedral carbon atom at flavin C(4) with a hydroxyl group attached to C(4). On the basis of the crystal structure of the borohydride-stabilized adduct, we conclude that the labile CPG-modified flavin is a 4a,5-dihydroflavin derivative with a substituent derived from the cleavage of the cyclopropyl ring in CPG. The results are consistent with CPG-mediated inactivation in a reaction initiated by single electron transfer from the amine function in CPG to FAD in MSOX, followed by collapse of the radical pair to yield a covalently modified 4a,5-dihydroflavin.
About this Structure
2A89 is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
Reference
Structure of the sodium borohydride-reduced N-(cyclopropyl)glycine adduct of the flavoenzyme monomeric sarcosine oxidase., Chen ZW, Zhao G, Martinovic S, Jorns MS, Mathews FS, Biochemistry. 2005 Nov 29;44(47):15444-50. PMID:16300392 Page seeded by OCA on Sat May 3 18:44:07 2008
