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| | ==Yeast polyamine oxidase FMS1, N195A mutant== | | ==Yeast polyamine oxidase FMS1, N195A mutant== |
| - | <StructureSection load='4gdp' size='340' side='right' caption='[[4gdp]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4gdp' size='340' side='right'caption='[[4gdp]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GDP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ech|4ech]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [https://pdbe.org/4gdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [https://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FMS1, YM9711.09, YMR020W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_polyamine_oxidase Non-specific polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.17 1.5.3.17] </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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [http://pdbe.org/4gdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [http://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST]] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref> | + | [https://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Non-specific polyamine oxidase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Adachi, M S]] | + | [[Category: Adachi MS]] |
| - | [[Category: Fitzpatrick, P F]] | + | [[Category: Fitzpatrick PF]] |
| - | [[Category: Hart, P J]] | + | [[Category: Hart PJ]] |
| - | [[Category: Taylor, A B]] | + | [[Category: Taylor AB]] |
| - | [[Category: Fad cofactor]]
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| - | [[Category: Flavoenzyme]]
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| - | [[Category: Mutant]]
| + | |
| - | [[Category: Oxidase]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
FMS1_YEAST Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.[1] [2]
Publication Abstract from PubMed
Flavoprotein Fms1 from Saccharomyces cerevisiae catalyzes the oxidation of spermine in the biosynthetic pathway for pantothenic acid. The same reaction is catalyzed by the mammalian polyamine and spermine oxidases. The active site of Fms1 contains three amino acid residues positioned to interact with the polyamine substrate, His67, Asn195, and Asp94. These three residues form a hydrogen-bonding triad with Asn195 being the central residue. Previous studies of the effects of mutating His67 are consistent with that residue being important both for interacting with the substrate and for maintaining the hydrogen bonds in the triad [Adachi, M. S., Taylor, A. B., Hart, P. J., and Fitzpatrick, P. F. (2012) Biochemistry 51, 4888-4897]. The N195A and D94N enzymes have now been characterized to evaluate their roles in catalysis. Both mutations primarily affect the reductive half-reaction. With N(1)-acetylspermine as the substrate, the rate constant for flavin reduction decreases approximately 450-fold for both mutations; the effects with spermine as the substrate are smaller, 20-40-fold. The k(cat)/K(amine)- and k(cat)-pH profiles with N(1)-acetylspermine are only slightly changed from the profiles for the wild-type enzyme, consistent with the pK(a) values arising from the amine substrate or product and not from active site residues. The structure of the N195A enzyme was determined at a resolution of 2.0 A. The structure shows a molecule of tetraethylene glycol in the active site and establishes that the mutation has no effect on the protein structure. Overall, the results are consistent with the role of Asn195 and Asp94 being to properly position the polyamine substrate for oxidation.
Mechanistic and Structural Analyses of the Roles of Active Site Residues in Yeast Polyamine Oxidase Fms1: Characterization of the N195A and D94N Enzymes.,Adachi MS, Taylor AB, Hart PJ, Fitzpatrick PF Biochemistry. 2012 Oct 15. PMID:23034052[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Landry J, Sternglanz R. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem Biophys Res Commun. 2003 Apr 11;303(3):771-6. PMID:12670477
- ↑ Chattopadhyay MK, Tabor CW, Tabor H. Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase. Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13869-74. Epub 2003 Nov 14. PMID:14617780 doi:http://dx.doi.org/10.1073/pnas.1835918100
- ↑ Adachi MS, Taylor AB, Hart PJ, Fitzpatrick PF. Mechanistic and Structural Analyses of the Roles of Active Site Residues in Yeast Polyamine Oxidase Fms1: Characterization of the N195A and D94N Enzymes. Biochemistry. 2012 Oct 15. PMID:23034052 doi:http://dx.doi.org/10.1021/bi3011434
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