Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant
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Structural constraints on protein self-processing in L-aspartate- -decarboxylaseStructural 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 †Role of the Sulfonium Center in Determining the Ligand Specificity of Human S -Adenosylmethionine DecarboxylaseComplexes ofThermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificityThreonine 57 is required for the post-translational activation ofEscherichia coliaspartate α-decarboxylaseCharacterization of a Novel Putative S-Adenosylmethionine Decarboxylase-Like Protein from Leishmania donovaniStructural biology of S-adenosylmethionine decarboxylase.Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase.Prediction and Analysis of Post-Translational Pyruvoyl Residue Modification Sites from Internal Serines in Proteins.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 accessCross-species activation of trypanosome S-adenosylmethionine decarboxylase by the regulatory subunit prozyme.S-Adenosylmethionine decarboxylase.Caenorhabditis elegans S-adenosylmethionine decarboxylase is highly stimulated by putrescine but exhibits a low specificity for activator binding.The activator-binding site of Onchocerca volvulus S-adenosylmethionine decarboxylase, a potential drug target.Polyamines and Their Role in Virus Infection.Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii.Mechanistic insights into the catalytic reaction of ferulic acid decarboxylase from Aspergillus niger: a QM/MM study.Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
P2860
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P2860
Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
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2001年論文
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2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
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name
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@ast
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@en
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@nl
type
label
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@ast
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@en
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@nl
prefLabel
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@ast
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@en
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@nl
P2093
P356
P1433
P1476
Structure of a human S-adenosy ...... s revealed by the H243A mutant
@en
P2093
P304
P356
10.1021/BI010736O
P407
P577
2001-08-01T00:00:00Z