Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity
10.1016/0378-1097(94)90478-2
Saved in:
Main Authors: | Tiow-Suan, S., Tan, D.S.H. |
---|---|
Other Authors: | MICROBIOLOGY |
Format: | Article |
Published: |
2016
|
Subjects: | |
Online Access: | http://scholarbank.nus.edu.sg/handle/10635/131247 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | National University of Singapore |
Similar Items
-
Mutational analysis of conserved glycines 42 and 256 in Cephalosporium acremonium isopenicillin N synthase
by: Loke, P., et al.
Published: (2012) -
Analysis of glutamines in catalysis in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis
by: Loke, P., et al.
Published: (2012) -
Catalytic activity in cephalosporium acremonium isopenicillin N synthase does not involve glutamine-234
by: Loke, P., et al.
Published: (2012) -
Mutational evidence for the role of serine-283 in Cephalosporium acremonium isopenicillin N synthase
by: Loke, P., et al.
Published: (2012) -
Mutational evidence for the role of serine-283 in Cephalosporium acremonium isopenicillin N synthase
by: Loke, P., et al.
Published: (2016)