Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties.
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Identification by virtual screening and in vitro testing of human DOPA decarboxylase inhibitorsLocal changes in the catalytic site of mammalian histidine decarboxylase can affect its global conformation and stabilityInternal proton transfer in the external pyridoxal 5'-phosphate Schiff base in dopa decarboxylase.Prediction of vitamin interacting residues in a vitamin binding protein using evolutionary information.Biogenic amines and polyamines: similar biochemistry for different physiological missions and biomedical applications.Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding.Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.Mapping of catalytically important residues in the rat L-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches.Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase.
P2860
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P2860
Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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name
Mutation of residues in the co ...... fects on catalytic properties.
@en
Mutation of residues in the co ...... fects on catalytic properties.
@nl
type
label
Mutation of residues in the co ...... fects on catalytic properties.
@en
Mutation of residues in the co ...... fects on catalytic properties.
@nl
prefLabel
Mutation of residues in the co ...... fects on catalytic properties.
@en
Mutation of residues in the co ...... fects on catalytic properties.
@nl
P2093
P2860
P1433
P1476
Mutation of residues in the co ...... fects on catalytic properties.
@en
P2093
C Bori Voltattorni
M Bertoldi
S Castellani
P2860
P304
P356
10.1046/J.1432-1327.2001.02187.X
P407
P577
2001-05-01T00:00:00Z