Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2.
about
A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basisIntegrative computational approach for genome-based study of microbial lipid-degrading enzymes.Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases.Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature.
P2860
Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@en
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@nl
type
label
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@en
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@nl
prefLabel
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@en
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@nl
P2093
P2860
P356
P1433
P1476
Homology modeling and active-s ...... lus acidocaldarius esterase 2.
@en
P2093
P2860
P304
P356
10.1110/PS.8.9.1789
P577
1999-09-01T00:00:00Z