4uqv
From Proteopedia
(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=4uqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqv RCSB], [http://www.ebi.ac.uk/pdbsum/4uqv PDBsum]</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=4uqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqv RCSB], [http://www.ebi.ac.uk/pdbsum/4uqv PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 20:09, 25 December 2014
methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP
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