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| | <StructureSection load='5fjr' size='340' side='right'caption='[[5fjr]], [[Resolution|resolution]] 2.44Å' scene=''> | | <StructureSection load='5fjr' size='340' side='right'caption='[[5fjr]], [[Resolution|resolution]] 2.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fjr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_sp. Amycolatopsis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FJR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fjr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_sp. Amycolatopsis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FJR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NPQ:N-ACETYL+NAPHTHYLALANINE'>NPQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.44Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fjo|5fjo]], [[5fjp|5fjp]], [[5fjt|5fjt]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NPQ:N-ACETYL+NAPHTHYLALANINE'>NPQ</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/o-succinylbenzoate_synthase o-succinylbenzoate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.113 4.2.1.113] </span></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=5fjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjr OCA], [https://pdbe.org/5fjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fjr RCSB], [https://www.ebi.ac.uk/pdbsum/5fjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjr ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjr OCA], [http://pdbe.org/5fjr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fjr RCSB], [http://www.ebi.ac.uk/pdbsum/5fjr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NSAR_AMYSP NSAR_AMYSP] Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-phenylglycine and N-succinyl-methionine (PubMed:14705949, PubMed:24955846). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-propionyl-D/L-methionine, N-butyryl-D/L-methionine and N-chloroacetyl-L-valine (PubMed:7766084, PubMed:10194342, PubMed:14705949, PubMed:23130969). Also converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342, PubMed:14705949, PubMed:24955846). Catalyzes both N-succinylamino acid racemization and OSB synthesis at equivalent rates (PubMed:14705949, PubMed:24955846). NSAR is probably the biological function of this enzyme (Probable).<ref>PMID:10194342</ref> <ref>PMID:14705949</ref> <ref>PMID:23130969</ref> <ref>PMID:24955846</ref> <ref>PMID:7766084</ref> <ref>PMID:16740275</ref> <ref>PMID:24955846</ref> |
| | + | == References == |
| | + | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Amycolatopsis sp]] | | [[Category: Amycolatopsis sp]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: O-succinylbenzoate synthase]]
| + | [[Category: Campopiano D]] |
| - | [[Category: Campopiano, D]] | + | [[Category: Grogan G]] |
| - | [[Category: Carron, G Sanchez]] | + | [[Category: Sanchez Carron G]] |
| - | [[Category: Grogan, G]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: N-acylamino acid]]
| + | |
| - | [[Category: Racemase]]
| + | |
| Structural highlights
Function
NSAR_AMYSP Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-phenylglycine and N-succinyl-methionine (PubMed:14705949, PubMed:24955846). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-propionyl-D/L-methionine, N-butyryl-D/L-methionine and N-chloroacetyl-L-valine (PubMed:7766084, PubMed:10194342, PubMed:14705949, PubMed:23130969). Also converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342, PubMed:14705949, PubMed:24955846). Catalyzes both N-succinylamino acid racemization and OSB synthesis at equivalent rates (PubMed:14705949, PubMed:24955846). NSAR is probably the biological function of this enzyme (Probable).[1] [2] [3] [4] [5] [6] [7]
References
- ↑ Palmer DR, Garrett JB, Sharma V, Meganathan R, Babbitt PC, Gerlt JA. Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase. Biochemistry. 1999 Apr 6;38(14):4252-8. PMID:10194342 doi:10.1021/bi990140p
- ↑ Taylor Ringia EA, Garrett JB, Thoden JB, Holden HM, Rayment I, Gerlt JA. Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis. Biochemistry. 2004 Jan 13;43(1):224-9. PMID:14705949 doi:10.1021/bi035815+
- ↑ Baxter S, Royer S, Grogan G, Brown F, Holt-Tiffin KE, Taylor IN, Fotheringham IG, Campopiano DJ. An Improved Racemase/Acylase Biotransformation for the Preparation of Enantiomerically Pure Amino Acids. J Am Chem Soc. 2012 Nov 15. PMID:23130969 doi:http://dx.doi.org/10.1021/ja305438y
- ↑ McMillan AW, Lopez MS, Zhu M, Morse BC, Yeo IC, Amos J, Hull K, Romo D, Glasner ME. Role of an active site loop in the promiscuous activities of Amycolatopsis sp. T-1-60 NSAR/OSBS. Biochemistry. 2014 Jul 15;53(27):4434-44. PMID:24955846 doi:10.1021/bi500573v
- ↑ Tokuyama S, Hatano K. Purification and properties of thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60. Appl Microbiol Biotechnol. 1995 Mar;42(6):853-9. PMID:7766084 doi:10.1007/BF00191181
- ↑ Glasner ME, Fayazmanesh N, Chiang RA, Sakai A, Jacobson MP, Gerlt JA, Babbitt PC. Evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase family of the enolase superfamily. J Mol Biol. 2006 Jun 30;360(1):228-50. PMID:16740275 doi:10.1016/j.jmb.2006.04.055
- ↑ McMillan AW, Lopez MS, Zhu M, Morse BC, Yeo IC, Amos J, Hull K, Romo D, Glasner ME. Role of an active site loop in the promiscuous activities of Amycolatopsis sp. T-1-60 NSAR/OSBS. Biochemistry. 2014 Jul 15;53(27):4434-44. PMID:24955846 doi:10.1021/bi500573v
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