Mechanism of human S-adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant
about
Structural constraints on protein self-processing in L-aspartate- -decarboxylaseCrystal Structure of Human Spermine Synthase: IMPLICATIONS OF SUBSTRATE BINDING AND CATALYTIC MECHANISMStructural Basis for Putrescine Activation of Human S -Adenosylmethionine Decarboxylase † ‡New Insights into the Design of Inhibitors of Human S -Adenosylmethionine Decarboxylase: Studies of Adenine C 8 Substitution in Structural Analogues of S -Adenosylmethionine †Complexes ofThermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificityThreonine 57 is required for the post-translational activation ofEscherichia coliaspartate α-decarboxylaseSpermine synthase.Structural biology of S-adenosylmethionine decarboxylase.Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase.The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A.Allosteric regulation of an essential trypanosome polyamine biosynthetic enzyme by a catalytically dead homologSingle-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme accessTrypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozymeGlycine enolates: the effect of formation of iminium ions to simple ketones on alpha-amino carbon acidity and a comparison with pyridoxal iminium ions.Relief of autoinhibition by conformational switch explains enzyme activation by a catalytically dead paralogPolyamine homoeostasis.S-Adenosylmethionine decarboxylase.The PLP cofactor: lessons from studies on model reactions.Functions of Polyamines in MammalsOverproduction of cardiac S-adenosylmethionine decarboxylase in transgenic mice.Species-Selective Pyrimidineamine Inhibitors of Trypanosoma brucei S-Adenosylmethionine Decarboxylase.Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
P2860
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P2860
Mechanism of human S-adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant
description
2003 nî lūn-bûn
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2003 թուականի Մարտին հրատարակուած գիտական յօդուած
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2003 թվականի մարտին հրատարակված գիտական հոդված
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2003年の論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年论文
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name
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@ast
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@en
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@nl
type
label
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@ast
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@en
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@nl
prefLabel
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@ast
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@en
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@nl
P2093
P356
P1433
P1476
Mechanism of human S-adenosylm ...... e structure of the S68A mutant
@en
P2093
Anthony E Pegg
Eric M Bennett
Jennifer L Ekstrom
Sarah E Cottet
Yang Zhang
P304
P356
10.1021/BI0268854
P407
P577
2003-03-04T00:00:00Z