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6a1h
From Proteopedia
(Difference between revisions)
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<StructureSection load='6a1h' size='340' side='right'caption='[[6a1h]], [[Resolution|resolution]] 1.36Å' scene=''> | <StructureSection load='6a1h' size='340' side='right'caption='[[6a1h]], [[Resolution|resolution]] 1.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6a1h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A1H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6a1h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_orientalis"_pittenger_and_brigham_1956 "streptomyces orientalis" pittenger and brigham 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A1H FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9O9:1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydropyrimido[4,5-b]quinolin-10(2H)-yl)-5-O-phosphono-D-ribitol'>9O9</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9O9:1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydropyrimido[4,5-b]quinolin-10(2H)-yl)-5-O-phosphono-D-ribitol'>9O9</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hmo ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31958 "Streptomyces orientalis" Pittenger and Brigham 1956])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxymandelate_oxidase 4-hydroxymandelate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.46 1.1.3.46] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxymandelate_oxidase 4-hydroxymandelate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.46 1.1.3.46] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a1h OCA], [http://pdbe.org/6a1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a1h RCSB], [http://www.ebi.ac.uk/pdbsum/6a1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a1h ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a1h OCA], [http://pdbe.org/6a1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a1h RCSB], [http://www.ebi.ac.uk/pdbsum/6a1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a1h ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/HMO_AMYOR HMO_AMYOR]] Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.<ref>PMID:11137816</ref> <ref>PMID:12240298</ref> | [[http://www.uniprot.org/uniprot/HMO_AMYOR HMO_AMYOR]] Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.<ref>PMID:11137816</ref> <ref>PMID:12240298</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Y128F single mutant of p-hydroxymandelate oxidase (Hmo) is capable of oxidizing mandelate to benzoate via a four-electron oxidative decarboxylation reaction. When benzoylformate (the product of the first two-electron oxidation) and hydrogen peroxide (an oxidant) were used as substrates the reaction did not proceed, suggesting that free hydrogen peroxide is not the committed oxidant in the second two-electron oxidation. How the flavin mononucleotide (FMN)-dependent four-electron oxidation reaction takes place remains elusive. Structural and biochemical explorations have shed new light on this issue. 15 high-resolution crystal structures of Hmo and its mutants liganded with or without a substrate reveal that oxidized FMN (FMNox) possesses a previously unknown electrophilic/nucleophilic duality. In the Y128F mutant the active-site perturbation ensemble facilitates the polarization of FMNox to a nucleophilic ylide, which is in a position to act on an alpha-ketoacid, forming an N5-acyl-FMNred dead-end adduct. In four-electron oxidation, an intramolecular disproportionation reaction via an N5-alkanol-FMNred C'alpha carbanion intermediate may account for the ThDP/PLP/NADPH-independent oxidative decarboxylation reaction. A synthetic 5-deaza-FMNox cofactor in combination with an alpha-hydroxyamide or alpha-ketoamide biochemically and structurally supports the proposed mechanism. | ||
| + | |||
| + | The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.,Lyu SY, Lin KH, Yeh HW, Li YS, Huang CM, Wang YL, Shih HW, Hsu NS, Wu CJ, Li TL Acta Crystallogr D Struct Biol. 2019 Oct 1;75(Pt 10):918-929. doi:, 10.1107/S2059798319011938. Epub 2019 Sep 24. PMID:31588923<ref>PMID:31588923</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6a1h" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Streptomyces orientalis pittenger and brigham 1956]] | ||
[[Category: 4-hydroxymandelate oxidase]] | [[Category: 4-hydroxymandelate oxidase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
Revision as of 07:02, 16 October 2019
Mandelate oxidase mutant-Y128F with 5-deazariboflavin mononucleotide
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