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Aminotransferase
From Proteopedia
(Difference between revisions)
| Line 51: | Line 51: | ||
**[[3hdo]] – HPA – ''Geobacter metallireducens''<br /> | **[[3hdo]] – HPA – ''Geobacter metallireducens''<br /> | ||
**[[4rae]] – MtHPA – ''Mycobacterium tuberculosis''<br /> | **[[4rae]] – MtHPA – ''Mycobacterium tuberculosis''<br /> | ||
| - | **[[4r8d]] – MtHPA + PLP <br /> | + | **[[4r8d]], [[5c6u]] – MtHPA + PLP <br /> |
*Ornithine aminotransferase | *Ornithine aminotransferase | ||
| Line 59: | Line 59: | ||
**[[2oat]] – hOA + PLP derivative <br /> | **[[2oat]] – hOA + PLP derivative <br /> | ||
**[[2byj]], [[2byl]] – hOA (mutant) + PLP <br /> | **[[2byj]], [[2byl]] – hOA (mutant) + PLP <br /> | ||
| + | **[[5eav]] – TgOA – ''Toxoplasma gondii'' <br /> | ||
| + | **[[5eqc]], [[4zwm]] – TgOA + PLP <br /> | ||
| + | **[[5e5i]] – TgOA + inactivator <br /> | ||
| + | **[[5e3k]] – TgOA + pentanoic acid derivative <br /> | ||
| + | **[[5dj9]] – TgOA + gabaculine<br /> | ||
*Acetylornithine aminotransferase | *Acetylornithine aminotransferase | ||
| Line 78: | Line 83: | ||
*Alanine glyoxylate aminotransferase | *Alanine glyoxylate aminotransferase | ||
| - | **[[1h0c]], [[2yob]] – hAGA + PLP <br /> | + | **[[1h0c]], [[2yob]], [[5f9s]] – hAGA + PLP <br /> |
**[[4cbr]], [[4cbs]] – hAGA (mutant) + PLP <br /> | **[[4cbr]], [[4cbs]] – hAGA (mutant) + PLP <br /> | ||
| - | **[[1j04]] – hAGA + PLP derivative <br /> | + | **[[1j04]], [[5hhy]] – hAGA + PLP derivative <br /> |
**[[4i8a]] – hAGA (mutant) + PLP derivative <br /> | **[[4i8a]] – hAGA (mutant) + PLP derivative <br /> | ||
**[[3r9a]] – hAGA + PLP derivative + peroxisomal targeting signal receptor<br /> | **[[3r9a]] – hAGA + PLP derivative + peroxisomal targeting signal receptor<br /> | ||
| Line 97: | Line 102: | ||
**[[5daa]] - BaAAT (mutant) + PLP derivative <br /> | **[[5daa]] - BaAAT (mutant) + PLP derivative <br /> | ||
**[[3lqs]] - BaAAT + thiophenecarboxylic acid<br /> | **[[3lqs]] - BaAAT + thiophenecarboxylic acid<br /> | ||
| + | **[[4m0j]] - BtAAT – ''Burkholderia thailandensis''<br /> | ||
| + | **[[4tm5]] - BtAAT + PLP <br /> | ||
*Branched chain amino acid aminotransferase | *Branched chain amino acid aminotransferase | ||
| Line 103: | Line 110: | ||
**[[1kt8]], [[1kta]] – hBCAT + PLP derivative <br /> | **[[1kt8]], [[1kta]] – hBCAT + PLP derivative <br /> | ||
**[[2alh]], [[5bwr]], [[5bwt]], [[5bwu]], [[5bwv]], [[5bwx]], [[5bww]], [[5cr5]] – hBCAT + PLP + inhibitor <br /> | **[[2alh]], [[5bwr]], [[5bwt]], [[5bwu]], [[5bwv]], [[5bwx]], [[5bww]], [[5cr5]] – hBCAT + PLP + inhibitor <br /> | ||
| + | **[[5i60]], [[5i5y]], [[5i5x]], [[5i5w]], [[5i5v]], [[5i5u]], [[5i5t]], [[5i5s]], [[5hne]] – hBCAT + PLP + biaryl amide<br /> | ||
**[[2hdk]], [[2hgw]], [[2hgx]], [[2hhf]] – hBCAT (mutant) + PLP <br /> | **[[2hdk]], [[2hgw]], [[2hgx]], [[2hhf]] – hBCAT (mutant) + PLP <br /> | ||
**[[2hg8]] – hBCAT (mutant) + PLP + methylleucine <br /> | **[[2hg8]] – hBCAT (mutant) + PLP + methylleucine <br /> | ||
| Line 109: | Line 117: | ||
**[[4cmd]] – NhBCAT + PLP – ''Nectria haematococca''<br /> | **[[4cmd]] – NhBCAT + PLP – ''Nectria haematococca''<br /> | ||
**[[4cmf]] – NhBCAT + inhibitor <br /> | **[[4cmf]] – NhBCAT + inhibitor <br /> | ||
| + | **[[5e25]] – BCAT + PLP + ketoglutarate – ''Geoglobus acetivorans'' <br /> | ||
| + | **[[5ce8]] – BCAT + PLP – ''Thermoproteus uzoniensis'' <br /> | ||
*Aromatic amino acid aminotransferase | *Aromatic amino acid aminotransferase | ||
| Line 170: | Line 180: | ||
**[[3r4t]] – GABA + PLP derivative – ''Mycobacterium marinum''<br /> | **[[3r4t]] – GABA + PLP derivative – ''Mycobacterium marinum''<br /> | ||
**[[4ffc]] – GABA + PLP derivative – ''Mycobacterium abscessus''<br /> | **[[4ffc]] – GABA + PLP derivative – ''Mycobacterium abscessus''<br /> | ||
| + | **[[4zsy]], [[4zsw]], [[4y0i]], [[4y0h]], [[4y0d]] – GABA + inactivator - pig <br /> | ||
*ArnB aminotransferase | *ArnB aminotransferase | ||
| Line 184: | Line 195: | ||
**[[3hbm]] - CjPseC (mutant)<br /> | **[[3hbm]] - CjPseC (mutant)<br /> | ||
**[[3hbn]] - CjPseC (mutant) + UDP<br /> | **[[3hbn]] - CjPseC (mutant) + UDP<br /> | ||
| + | |||
| + | *TlmJ aminotransferase | ||
| + | |||
| + | **[[5uid]] - TlmJ + PLP – ''Streptoalloteichus hindustanus''<br /> | ||
*WbpE aminotransferase | *WbpE aminotransferase | ||
| Line 191: | Line 206: | ||
**[[3nyt]] - PaWbpE (mutant) + PLP derivative<br /> | **[[3nyt]] - PaWbpE (mutant) + PLP derivative<br /> | ||
| - | *Alpha- | + | *Alpha-aminoadipate aminotransferase |
| - | **[[2egy]] - TtLysN + PLP <br /> | + | **[[2egy]], [[5eun]] - TtLysN + PLP <br /> |
**[[3cbf]], [[2zyj]] - TtLysN + PLP derivative<br /> | **[[3cbf]], [[2zyj]] - TtLysN + PLP derivative<br /> | ||
**[[2zp7]], [[2z1y]] - TtLysN + PLP + leucine<br /> | **[[2zp7]], [[2z1y]] - TtLysN + PLP + leucine<br /> | ||
| + | **[[5tf5]] - hLysN + PLP derivative + inhibitor<br /> | ||
| + | **[[5efs]] - hLysN II <br /> | ||
| + | |||
| + | *Broad specificity aminotransferase | ||
| + | |||
| + | **[[4wb0]] - BsAT – Leishmania mexicana<br /> | ||
| + | |||
| + | *Adenosylmethionine-8-amino-7-oxononanoate aminotransferase | ||
| + | **[[4w1x]], [[4w1w]], [[4w1v]], [[4xjl]], [[4xjm]], [[4xjo]], [[4xjp]] - MtDAPA + PLP + inhibitor<br /> | ||
| + | **[[4mqr]], [[4mqq]], [[4mqp]] - MtDAPA + inhibitor<br /> | ||
| + | **[[5uc7]] - DAPA + PLP derivative – ''Citrobacter rodentium''<br /> | ||
| + | *Putrescine aminotransferase | ||
| + | **[[4uoy]] - EcPAT + PLP <br /> | ||
| + | **[[4uox]] - EcPAT + PLP + putrescine<br /> | ||
| + | *Omega amino acid-pyruvate aminotransferase | ||
| + | **[[4uho]], [[4uhn]], [[4uhm]] - PaOAAT + PLP <br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:31, 5 March 2017
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3D structures of aminotransferase
Updated on 05-March-2017
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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