Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.
Human carbonyl reductase is a member of the short-chain dehydrogenase/reductase (SDR) protein superfamily and is known to play an important role in the detoxification of xenobiotics bearing a carbonyl group. The two monomeric NADPH-dependent human isoforms of cytosolic carbonyl reductase CBR1 and CB...
Prif Awduron: | El-Hawari, Y, Favia, A, Pilka, E, Kisiela, M, Oppermann, U, Martin, H, Maser, E |
---|---|
Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
2009
|
Pynciau: |
Eitemau Tebyg
-
Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.
gan: El-Hawari, Y, et al.
Cyhoeddwyd: (2009) -
Comprehensive site-directed mutagenesis of L-2-Halo acid dehalogenase to probe catalytic amino acid residues/
gan: 497336 Kurihara, Tatsuo, et al. -
Characterization of the human carbonyl reductase 3 (CBR3) by site-directed mutagenesis
gan: El-Hawari, Y, et al.
Cyhoeddwyd: (2008) -
Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues/
gan: 497336 Kurihara, Tatsuo, et al. -
REMP software to introduce a screening REstriction site in site-directed Mutagenesis Primer
gan: Madhavi Latha Yadav Bangaru, PhD, et al.
Cyhoeddwyd: (2021-12-01)