4oma: Difference between revisions

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<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=4oma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oma RCSB], [http://www.ebi.ac.uk/pdbsum/4oma PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

MGL catalyzes the gamma-elimination of L-methionine and its derivatives as well as the beta-elimination of L-cysteine and its analogs. These reactions yield alpha-keto acids and thiols. The mechanism of chemical conversion of amino acids includes numerous reaction intermediates. The detailed analysis of MGL interaction with glycine, L-alanine, L-norvaline and L-cycloserine was performed by pre-steady-state stopped-flow kinetics. The structure of side chains of the amino acids is important both for their binding with enzyme and for the stability of the external aldimine and ketimine intermediates. X-ray structure of MGL-L-cycloserine complex has been solved at 1.6 A resolution. The structure models ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediates interconversion at the stages of external aldimine and ketimine formation.

Pre-Steady-State Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.,Kuznetsov NA, Faleev NG, Kuznetsova AA, Morozova EA, Revtovich SV, Anufrieva NV, Nikulin AD, Fedorova OS, Demidkina TV J Biol Chem. 2014 Nov 14. pii: jbc.M114.586511. PMID:25398880<ref>PMID:25398880</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 8: / Line 8: @@
 <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=4oma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oma RCSB], [http://www.ebi.ac.uk/pdbsum/4oma PDBsum]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+MGL catalyzes the gamma-elimination of L-methionine and its derivatives as well as the beta-elimination of L-cysteine and its analogs. These reactions yield alpha-keto acids and thiols. The mechanism of chemical conversion of amino acids includes numerous reaction intermediates. The detailed analysis of MGL interaction with glycine, L-alanine, L-norvaline and L-cycloserine was performed by pre-steady-state stopped-flow kinetics. The structure of side chains of the amino acids is important both for their binding with enzyme and for the stability of the external aldimine and ketimine intermediates. X-ray structure of MGL-L-cycloserine complex has been solved at 1.6 A resolution. The structure models ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediates interconversion at the stages of external aldimine and ketimine formation.
+Pre-Steady-State Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.,Kuznetsov NA, Faleev NG, Kuznetsova AA, Morozova EA, Revtovich SV, Anufrieva NV, Nikulin AD, Fedorova OS, Demidkina TV J Biol Chem. 2014 Nov 14. pii: jbc.M114.586511. PMID:25398880<ref>PMID:25398880</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>