Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability

scientific article

Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.BBAPAP.2008.09.007
P698PubMed publication ID18930847

P2093author name stringYan Feng
Baisong Zheng
Le Gao
Guangyu Yang
Zuoming Zhang
Aixi Bai
P433issue1
P304page(s)94-102
P577publication date2008-10-01
P1433published inBiochimica et Biophysica ActaQ864239
P1476titleGlu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability
P478volume1794

Reverse relations

cites work (P2860)
Q43016806Alteration of substrate specificities of thermophilic α/β hydrolases through domain swapping and domain interface optimization
Q84128601Amino acid substitutions in the N-terminus, cord and α-helix domains improved the thermostability of a family 11 xylanase XynR8
Q37526646Carboxylic ester hydrolases from hyperthermophiles.
Q27681416Enhanced Enzyme Kinetic Stability by Increasing Rigidity within the Active Site
Q52810253Exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations.
Q28076256Marine Microbiological Enzymes: Studies with Multiple Strategies and Prospects
Q31060831Mechanisms of intramolecular communication in a hyperthermophilic acylaminoacyl peptidase: a molecular dynamics investigation
Q39556441Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos
Q34606653Reciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila.
Q36922673Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering.
Q47254850Understanding the interactions of different substrates with wild-type and mutant acylaminoacyl peptidase using molecular dynamics simulations

Search more.