[The effect of point amino acid substitutions in an internal alpha-helix on thermostability of Aspergillus awamori X100 glucoamylase].
Conformational flexibility of alpha-helices in glucoamylase of the fungus Aspergillus awamori was studied by molecular dynamics methods. Several amino acid substitutions (G127A, P128A, I136L, G137A, and G139A) optimizing intrinsic interactions in one of the alpha-helices (D) within the hydrophobic core of this protein were constructed and studied. It was found that these point mutations had different effects on the glucoamylase thermal inactivation constant. Unlike amino acid substitution P128A and substitutions G137A and A246C, I136L and G139A displayed a pronounced additive thermostabilizing effect.
Surzhik
M A
MA
Churkina
S V
SV
Shmidt
A E
AE
Shvetsov
A V
AV
Kozhina
T N
TN
Firsov
D L
DL
Firsov
L M
LM
Petukhov
M G
MG
D019943:Amino Acid Substitution; D001230:Aspergillus / Q000201:enzymology*; D004795:Enzyme Stability / Q000235:genetics; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry / Q000235:genetics*; D017354:Point Mutation; D017433:Protein Structure, Secondary
D005087:Glucan 1,4-alpha-Glucosidase