Aminotransferase
From Proteopedia
(Difference between revisions)
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The <scene name='72/721044/Cv/3'>active site of histidinol-phosphate aminotransferase contains PLP</scene>.<ref>PMID:11294630</ref> | The <scene name='72/721044/Cv/3'>active site of histidinol-phosphate aminotransferase contains PLP</scene>.<ref>PMID:11294630</ref> | ||
+ | ==3D structures of aminotransferase== | ||
+ | [[Aminotransferase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[3hdo]] – HPA – ''Geobacter metallireducens''<br /> | **[[3hdo]] – HPA – ''Geobacter metallireducens''<br /> | ||
**[[4rae]] – MtHPA – ''Mycobacterium tuberculosis''<br /> | **[[4rae]] – MtHPA – ''Mycobacterium tuberculosis''<br /> | ||
- | **[[4r8d]], [[5c6u]] – MtHPA + PLP <br /> | + | **[[4r8d]], [[5c6u]], [[5yhv]] – MtHPA + PLP <br /> |
*Ornithine aminotransferase | *Ornithine aminotransferase | ||
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**[[4cmd]] – NhBCAT + PLP – ''Nectria haematococca''<br /> | **[[4cmd]] – NhBCAT + PLP – ''Nectria haematococca''<br /> | ||
**[[4cmf]] – NhBCAT + inhibitor <br /> | **[[4cmf]] – NhBCAT + inhibitor <br /> | ||
- | **[[ | + | **[[5cm0]] – GaBCAT + PLP – ''Geoglobus acetivorans'' <br /> |
+ | **[[5e25]] – GaBCAT + PLP + ketoglutarate <br /> | ||
**[[5ce8]] – BCAT + PLP – ''Thermoproteus uzoniensis'' <br /> | **[[5ce8]] – BCAT + PLP – ''Thermoproteus uzoniensis'' <br /> | ||
**[[5u3f]] – MtBCAT + cycloserine <br /> | **[[5u3f]] – MtBCAT + cycloserine <br /> | ||
+ | **[[6nst]] - BCAT – ''Pseudomonas aeruginosa''<br /> | ||
+ | **[[6gkr]] – TtBCAT + PLP – ''Thermobaculum terrenum'' <br /> | ||
+ | **[[6q8e]] – TtBCAT + PLP derivative <br /> | ||
+ | **[[6h65]] – TtBCAT + PLP – ''Haliangium ochraceum'' <br /> | ||
+ | **[[4whx]] – BCAT + PLP – ''Burkholderia pseudomallei'' <br /> | ||
*Aromatic amino acid aminotransferase | *Aromatic amino acid aminotransferase | ||
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**[[4rkc]] – PsAROAT + PLP derivative - ''Psychrobacter''<br /> | **[[4rkc]] – PsAROAT + PLP derivative - ''Psychrobacter''<br /> | ||
**[[4rkd]] – PsAROAT + PLP derivative + PLP<br /> | **[[4rkd]] – PsAROAT + PLP derivative + PLP<br /> | ||
+ | **[[6hnb]] – CaAROAT – ''Candida albicans'' <br /> | ||
+ | **[[6hnu]] – CaAROAT + PLP + Phe<br /> | ||
*Tyrosine aminotransferase | *Tyrosine aminotransferase | ||
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**[[3ihj]] – hALAAT 2 + PLP <br /> | **[[3ihj]] – hALAAT 2 + PLP <br /> | ||
**[[3tcm]] – ALAAT 2 (mutant) + PLP derivative - barley<br /> | **[[3tcm]] – ALAAT 2 (mutant) + PLP derivative - barley<br /> | ||
+ | |||
+ | *Cysteine aminotransferase | ||
+ | |||
+ | **[[4w91]] – CYSAT + PLP – ''Brucella suis''<br /> | ||
*Glutamine aminotransferase | *Glutamine aminotransferase | ||
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*WbpE aminotransferase | *WbpE aminotransferase | ||
- | **[[3nu7]], [[3nu8]], [[3nub]], [[3nyu]] - PaWbpE + PLP derivative | + | **[[3nu7]], [[3nu8]], [[3nub]], [[3nyu]] - PaWbpE + PLP derivative <br /> |
**[[3nys]] - PaWbpE (mutant) + PLP <br /> | **[[3nys]] - PaWbpE (mutant) + PLP <br /> | ||
**[[3nyt]] - PaWbpE (mutant) + PLP derivative<br /> | **[[3nyt]] - PaWbpE (mutant) + PLP derivative<br /> | ||
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*C-6’ aminotransferase | *C-6’ aminotransferase | ||
- | **[[6cbo]] - | + | **[[6cbo]] - MeAT – ''Micromonospora echinospora'' <br /> |
+ | **[[5z83]] – MeAT + PLP <br /> | ||
+ | **[[5z8a]] – MeAT + PLP + JI-20A <br /> | ||
+ | **[[5z8k]] – MeAT + PLP + neomycin <br /> | ||
*Kynurenine aminotransferase | *Kynurenine aminotransferase | ||
- | **[[ | + | **[[4wlh]], [[4wlj]], [[4wp0]] – hKAT 1 + PLP derivative <br /> |
- | + | **[[5efs]], [[6d0a]] – hKAT 2 <br /> | |
- | **[[ | + | |
- | + | ||
**[[5tf5]] – hKAT 2 + PLP derivative + inhibitor<br /> | **[[5tf5]] – hKAT 2 + PLP derivative + inhibitor<br /> | ||
+ | **[[5vep]], [[5veq]], [[5ver]] – mKAT 3 + PLP derivative <br /> | ||
+ | **[[5veh]] – AaKAT + PLP derivative <br /> | ||
+ | |||
+ | *Diaminopelargonic acid aminotransferase | ||
+ | |||
+ | **[[6erk]] – DPAAT + PLP – ''Psychrobacter cryohalolentis'' <br /> | ||
+ | |||
+ | *D-phenylglycine aminotransferase | ||
+ | |||
+ | **[[6dvs]] – DPGAT – ''Pseudomonas stutzeri'' <br /> | ||
+ | |||
+ | *Aminotransferase class II | ||
+ | |||
+ | **[[5z0q]] – AT2 + PLP – ''Erwinia tasmaniensis'' <br /> | ||
*Aminotransferase class III | *Aminotransferase class III |
Revision as of 08:56, 14 March 2019
|
3D structures of aminotransferase
Updated on 14-March-2019
References
- ↑ Mizuguchi H, Hayashi H, Miyahara I, Hirotsu K, Kagamiyama H. Characterization of histidinol phosphate aminotransferase from Escherichia coli. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):321-4. PMID:12686152
- ↑ Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol. 1984 Apr 15;174(3):497-525. PMID:6143829 doi:http://dx.doi.org/10.1016/0022-2836(84)90333-4
- ↑ Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol. 1984 Apr 15;174(3):497-525. PMID:6143829 doi:http://dx.doi.org/10.1016/0022-2836(84)90333-4
- ↑ Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H. Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Biochemistry. 2001 Apr 17;40(15):4633-44. PMID:11294630
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