Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins
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Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases.Structure-function correlations in tyrosinasesTyrosinase versus Catechol Oxidase: One Asparagine Makes the DifferenceRepositioning of Thiourea-Containing Drugs as Tyrosinase InhibitorsImmunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.The structure of a prophenoloxidase (PPO) from Anopheles gambiae provides new insights into the mechanism of PPO activationEnzymatic browning in avocado (Persea americana) revisited: History, advances and future perspectives.Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases.Activation of dioxygen by copper metalloproteins and insights from model complexes.Re-evaluation of insect melanogenesis research: Views from the dark side.The albinism of the feral Asinara white donkeys (Equus asinus) is determined by a missense mutation in a highly conserved position of the tyrosinase (TYR) gene deduced protein.The unravelling of the complex pattern of tyrosinase inhibition.The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of "Substrate-Guiding Residues" for Enzymatic Specificity.Latent and active aurone synthase from petals of C. grandiflora: a polyphenol oxidase with unique characteristics.Structural and kinetic considerations on the catalysis of deoxyarbutin by tyrosinase.Kinetic characterization of substrate-analogous inhibitors of tyrosinase.A specific amino acid residue in the catalytic site of dandelion polyphenol oxidases acts as 'selector' for substrate specificity.The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One.4-n-butylresorcinol, a depigmenting agent used in cosmetics, reacts with tyrosinase.Thiopurine Drugs Repositioned as Tyrosinase Inhibitors.On the Metal Cofactor in the Tyrosinase Family.Heterologous expression of tyrosinase (MelC2) from Streptomyces avermitilis MA4680 in E. coli and its application for ortho-hydroxylation of resveratrol to produce piceatannol.pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases
P2860
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P2860
Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins
description
2014 nî lūn-bûn
@nan
2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Determination of tyrosinase su ...... between type-3 copper proteins
@ast
Determination of tyrosinase su ...... between type-3 copper proteins
@en
Determination of tyrosinase su ...... between type-3 copper proteins
@nl
type
label
Determination of tyrosinase su ...... between type-3 copper proteins
@ast
Determination of tyrosinase su ...... between type-3 copper proteins
@en
Determination of tyrosinase su ...... between type-3 copper proteins
@nl
prefLabel
Determination of tyrosinase su ...... between type-3 copper proteins
@ast
Determination of tyrosinase su ...... between type-3 copper proteins
@en
Determination of tyrosinase su ...... between type-3 copper proteins
@nl
P2093
P2860
P3181
P356
P1476
Determination of tyrosinase su ...... between type-3 copper proteins
@en
P2093
Margarita Kanteev
Mor Goldfeder
Sivan Isaschar-Ovdat
P2860
P2888
P3181
P356
10.1038/NCOMMS5505
P407
P577
2014-07-30T00:00:00Z
P5875
P6179
1023703100