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-Structure paper
Title | Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis. |
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Journal, issue, pages | J. Biol. Chem., Vol. 296, Page 100797-100797, Year 2021 |
Publish date | Oct 1, 2020 (structure data deposition date) |
![]() | Brewster, J.L. / Pachl, P. / McKellar, J.L.O. / Selmer, M. / Squire, C.J. / Patrick, W.M. |
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Methods | X-ray diffraction |
Resolution | 1.85 Å |
Structure data | ![]() PDB-7kb0: ![]() PDB-7kb1: |
Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-WBJ: ![]() ChemComp-NA: ![]() ChemComp-PGE: ![]() ChemComp-PLP: ![]() ChemComp-MG: |
Source |
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![]() | TRANSFERASE / Thermotoga maritima / methionine biosynthesis / enzyme kinetics / O-acety-L-homoserine aminocarboxypropyltransferase / MetY / active site |