2a89

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(New page: 200px<br /><applet load="2a89" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a89, resolution 1.85&Aring;" /> '''Monomeric Sarcosine ...)
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'''Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme'''<br />
'''Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2A89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with PO4, CL and FCG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sarcosine_oxidase Sarcosine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.1 1.5.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A89 OCA].
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2A89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=FCG:'>FCG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sarcosine_oxidase Sarcosine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.1 1.5.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A89 OCA].
==Reference==
==Reference==
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[[Category: Sarcosine oxidase]]
[[Category: Sarcosine oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chen, Z.W.]]
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[[Category: Chen, Z W.]]
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[[Category: Jorns, M.S.]]
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[[Category: Jorns, M S.]]
[[Category: Martinovic, S.]]
[[Category: Martinovic, S.]]
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[[Category: Mathews, F.S.]]
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[[Category: Mathews, F S.]]
[[Category: Zhao, G.]]
[[Category: Zhao, G.]]
[[Category: CL]]
[[Category: CL]]
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[[Category: oxidase]]
[[Category: oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:34 2008''

Revision as of 14:24, 21 February 2008


2a89, resolution 1.85Å

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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. with , and as ligands. Active as Sarcosine oxidase, with EC number 1.5.3.1 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

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