Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.
about
Computational enzyme design approaches with significant biological outcomes: progress and challengesHuman Naa50 Protein Displays Broad Substrate Specificity for Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL ANALYSIS USING TETRAPEPTIDE LIBRARY.The unique functional role of the C-HS hydrogen bond in the substrate specificity and enzyme catalysis of type 1 methionine aminopeptidase.Structure-guided systems-level engineering of oxidation-prone methionine residues in catalytic domain of an alkaline α-amylase from Alkalimonas amylolytica for significant improvement of both oxidative stability and catalytic efficiencyStructural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.
P2860
Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.
description
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name
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@en
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@nl
type
label
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@en
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@nl
prefLabel
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@en
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@nl
P2093
P2860
P356
P1433
P1476
Glu121-Lys319 salt bridge betw ...... erichia coli aminopeptidase N.
@en
P2093
Anthony Addlagatta
Chandan Kishor
Nishant Jain
Rajesh Gumpena
Roopa Jones Ganji
P2860
P304
P356
10.1002/PRO.2060
P577
2012-03-30T00:00:00Z