Structural basis and mechanism of the inhibition of the type-3 copper protein tyrosinase from Streptomyces antibioticus by halide ions.
about
Characterization of SLAC: a small laccase from Streptomyces coelicolor with unprecedented activity.Design and discovery of mushroom tyrosinase inhibitors and their therapeutic applications.Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme.Modeling the met form of human tyrosinase: a refined and hydrated pocket for antagonist design.Effect of Cl- on tyrosinase: complex inhibition kinetics and biochemical implication.Tyrosinase-catalyzed oxidation of fluorophenols.Characterization of the zinc-binding site of the histidine-proline-rich glycoprotein associated with rabbit skeletal muscle AMP deaminase.Substrate inhibition competes with halide inhibition in polyphenol oxidase.Copper (II) binding of NAD(P)H- flavin oxidoreductase (NfoR) enhances its Cr (VI)-reducing ability.Stopped-flow fluorescence studies of inhibitor binding to tyrosinase from Streptomyces antibioticus.
P2860
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P2860
Structural basis and mechanism of the inhibition of the type-3 copper protein tyrosinase from Streptomyces antibioticus by halide ions.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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2002年学术文章
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name
Structural basis and mechanism ...... s antibioticus by halide ions.
@en
Structural basis and mechanism ...... s antibioticus by halide ions.
@nl
type
label
Structural basis and mechanism ...... s antibioticus by halide ions.
@en
Structural basis and mechanism ...... s antibioticus by halide ions.
@nl
prefLabel
Structural basis and mechanism ...... s antibioticus by halide ions.
@en
Structural basis and mechanism ...... s antibioticus by halide ions.
@nl
P2860
P356
P1476
Structural basis and mechanism ...... s antibioticus by halide ions.
@en
P2093
Armand W J W Tepper
Gerard W Canters
P2860
P304
30436-30444
P356
10.1074/JBC.M202461200
P407
P577
2002-06-04T00:00:00Z