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