| http://purl.uniprot.org/citations/16300392 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16300392 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0515422"xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/author | "Mathews F.S."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/author | "Zhao G."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/author | "Chen Z.W."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/author | "Jorns M.S."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/author | "Martinovic S."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/pages | "15444-15450"xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/title | "Structure of the sodium borohydride-reduced N-(cyclopropyl)glycine adduct of the flavoenzyme monomeric sarcosine oxidase."xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://purl.uniprot.org/core/volume | "44"xsd:string |
| http://purl.uniprot.org/citations/16300392 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16300392 |
| http://purl.uniprot.org/citations/16300392 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16300392 |
| http://purl.uniprot.org/uniprot/#_P40859-mappedCitation-16300392 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16300392 |
| http://purl.uniprot.org/uniprot/P40859 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/16300392 |