A Thioester Substrate Binds to the Enzyme Arthrobacter Thioesterase in Two Ionization States; Evidence from Raman Difference Spectroscopy
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The Catalytic Mechanism of the Hotdog-fold Enzyme Superfamily 4-Hydroxybenzoyl-CoA Thioesterase from Arthrobacter sp. Strain SUStructure and Catalysis in the Escherichia coli Hotdog-fold Thioesterase Paralogs YdiI and YbdBActive site comparisons and catalytic mechanisms of the hot dog superfamily.Green and Sustainable Technology for High-Efficiency and Low-Damage Manipulation of Densely Crosslinked Proteins.
P2860
A Thioester Substrate Binds to the Enzyme Arthrobacter Thioesterase in Two Ionization States; Evidence from Raman Difference Spectroscopy
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name
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@ast
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@en
type
label
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@ast
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@en
prefLabel
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@ast
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@en
P2093
P2860
P356
P1476
A Thioester Substrate Binds to ...... Raman Difference Spectroscopy
@en
P2093
Debra Dunaway-Mariano
Paul R Carey
P2860
P356
10.1002/JRS.3002
P577
2012-01-01T00:00:00Z