Aspartate decarboxylase

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<StructureSection load='1uhd' size='340' side='right' caption='Structure of aspartate decarboxylase α (grey) and β (green) subunits complex with pyruvate (PDB code [[1uhd]]).' scene=''>
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<StructureSection load='1uhd' size='340' side='right' caption='Structure of aspartate decarboxylase α (green) and β (magenta) subunits complex with pyruvate (PDB code [[1uhd]]).' scene='59/592671/Cv/1'>
== Function ==
== Function ==
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'''Aspartate 1-decarboxylase''' or '''aspartate α-decarboxylase''' (AADC) catalyzes the conversion of L-aspartate to β-alanine and CO2. '''Aspartate 4-decarboxylase''' or '''aspartate β-decarboxylase''' (ABDC) catalyzes the conversion of L-aspartate to L-alanine and CO2. AADC is a pyruvate-dependent enzyme which is synthesized as an inactive protein. The AADC inactive precursor is cleaved to the active α and β subunits. ABDC is a pyridoxal-5’-phosphate (PLP)-dependent enzyme.
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'''Aspartate 1-decarboxylase''' or '''aspartate α-decarboxylase''' (AADC) catalyzes the conversion of L-aspartate to β-alanine and CO2.<ref>PMID:14633979</ref> '''Aspartate 4-decarboxylase''' or '''aspartate β-decarboxylase''' (ABDC) catalyzes the conversion of L-aspartate to L-alanine and CO2.<ref>PMID:19368885</ref> AADC is a pyruvate-dependent enzyme which is synthesized as an inactive protein. The AADC inactive precursor is cleaved to the active α and β subunits. ABDC is a pyridoxal-5’-phosphate (PLP)-dependent enzyme.
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*<scene name='59/592671/Cv/3'>Pyruvate binding site</scene> of AADC (PDB code [[1uhd]]).<ref>PMID:15184017</ref>
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</StructureSection>
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==3D structures of aspartate decarboxylase==
==3D structures of aspartate decarboxylase==
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[[Aspartate decarboxylase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*Aspartate α-decarboxylase
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</StructureSection>
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**[[1aw8]], [[1pt0]], [[1pyq]] – EcAADC – ''Escherichia coli''<br />
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**[[1pt1]], [[1pqe]], [[1pqf]], [[1pqh]], [[1pyu]], [[3tm7]], [[4azd]] – EcAADC (mutant)<br />
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**[[1ppy]] – EcAADC precursor<br />
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**[[1vc3]] – TtAADC – ''Thermus thermophilus''<br />
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**[[2c45]] – AADC – ''Mycobacterium tuberculosis''<br />
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**[[3oug]] – AADC – ''Francesella tularensis''<br />
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**[[3plx]] – AADC – ''Campylobacter jejuni'' <br />
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*Aspartate α-decarboxylase complexes
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**[[1uhd]] – HpAADC + pyruvate – ''Helicobacter pylori''<br />
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**[[1uhe]] – HpAADC + isoasparagine<br />
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**[[2eeo]] – TtAADC + pyruvate + fumarate<br />
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**[[4aok]], [[4aon]] – EcAADC + methyl aspartate derivative<br />
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*Aspartate β-decarboxylase
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**[[2zy2]], [[3fdd]] – ABDC + PLP – ''Pseudomonas''<br />
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**[[2zy3]], [[2zy4]] – AfABDC + PLP – ''Alcaligenes faecalis''<br />
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**[[2zy5]] – AfABDC (mutant) +PLP<br />
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}}
 
== References ==
== References ==

Current revision

Structure of aspartate decarboxylase α (green) and β (magenta) subunits complex with pyruvate (PDB code 1uhd).

Drag the structure with the mouse to rotate


References

  1. ↑ Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL. Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase. EMBO J. 2003 Dec 1;22(23):6193-204. PMID:14633979 doi:10.1093/emboj/cdg575
  2. ↑ Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH. Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase. Structure. 2009 Apr 15;17(4):517-29. PMID:19368885 doi:10.1016/j.str.2009.02.013
  3. ↑ Lee BI, Suh SW. Crystal structure of the schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase. J Mol Biol. 2004 Jun 25;340(1):1-7. PMID:15184017 doi:10.1016/j.jmb.2004.04.049

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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