TY - JOUR
T1 - 1H, 13C and 15N resonance assignments of wild-type Bacillus subtilis Lipase A and its mutant evolved towards thermostability
AU - Augustyniak, W.
AU - Wienk, H.L.J.
AU - Boelens, R.
AU - Reetz, M.T.
PY - 2013
Y1 - 2013
N2 - Previously, we evolved Lipase A from Bacillus
subtilis towards increased thermostability. The resulting
mutant retains significant catalytic activity upon heating
above 60 C (and up to 100 C) and cooling down, whereas
wild-type lipase precipitates irreversibly and does not show
significant activity in these conditions. Kinetic thermostability
of proteins has not been characterized well on the
molecular structure level so far, therefore our aim is to study
it using NMR spectroscopy. Here, nearly complete 1H, 13C
and 15N resonance assignments are reported for wild-type
and mutant Lipase A. Chemical shifts were used to predict
secondary structure elements of both Lipase A variants.
AB - Previously, we evolved Lipase A from Bacillus
subtilis towards increased thermostability. The resulting
mutant retains significant catalytic activity upon heating
above 60 C (and up to 100 C) and cooling down, whereas
wild-type lipase precipitates irreversibly and does not show
significant activity in these conditions. Kinetic thermostability
of proteins has not been characterized well on the
molecular structure level so far, therefore our aim is to study
it using NMR spectroscopy. Here, nearly complete 1H, 13C
and 15N resonance assignments are reported for wild-type
and mutant Lipase A. Chemical shifts were used to predict
secondary structure elements of both Lipase A variants.
U2 - 10.1007/s12104-012-9420-z
DO - 10.1007/s12104-012-9420-z
M3 - Article
SN - 1874-270X
VL - 7
SP - 249
EP - 252
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
ER -