Pseudomonas putida PqqB with a non-physiological zinc at the active site binds the substrate mimic, 5-cysteinyl-3,4-dihydroxyphenylalanine (5-Cys-DOPA), non-specifically but supports the proposed function of the enzyme in pyrroloquinoline quinone biosynthesis.
收藏Protein Data Bank Japan2024-03-13 更新2026-03-21 收录
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Pseudomonas putida PqqB with a non-physiological zinc at the active site binds the substrate mimic, 5-cysteinyl-3,4-dihydroxyphenylalanine (5-Cys-DOPA), non-specifically but supports the proposed function of the enzyme in pyrroloquinoline quinone biosynthesis. Descriptor: 3-{[(2S)-2-amino-2-carboxyethyl]sulfanyl}-5-hydroxy-L-tyrosine, CHLORIDE ION, Coenzyme PQQ synthesis protein B, ... Authors: Evans III, R.L, Wilmot, C.M. Deposit date: 2018-07-09 Release date: 2019-05-22 Last modified: 2024-03-13 Method: X-RAY DIFFRACTION (2.349 Å) Cite: Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway. J.Am.Chem.Soc., 141, 2019
创建时间：
2018-07-09
