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3aaw
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=3aaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaw RCSB], [http://www.ebi.ac.uk/pdbsum/3aaw 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=3aaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaw RCSB], [http://www.ebi.ac.uk/pdbsum/3aaw PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/AK_CORGL AK_CORGL]] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.<ref>PMID:17350037</ref> <ref>PMID:20573952</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 05:07, 25 December 2014
Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine
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Categories: Aspartate kinase | Corynebacterium crenatum | Corynebacterium glutamicum | Kuzuyama, T | Nishiyama, M | Tomita, T | Yoshida, A | Alternative initiation | Amino-acid biosynthesis | Atp-binding | Concerted inhibition | Diaminopimelate biosynthesis | Kinase | Lysine biosynthesis | Nucleotide-binding | Transferase
