Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334-->Gly mutant enzymes.
about
Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzymeAsn124 of Cel5A from Hypocrea jecorina not only provides the N-glycosylation site but is also essential in maintaining enzymatic activityInterplay of catalytic subsite residues in the positioning of α-d-glucose 1-phosphate in sucrose phosphorylase.The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose.
P2860
Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334-->Gly mutant enzymes.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Probing the active site of Cor ...... d His334-->Gly mutant enzymes.
@en
type
label
Probing the active site of Cor ...... d His334-->Gly mutant enzymes.
@en
prefLabel
Probing the active site of Cor ...... d His334-->Gly mutant enzymes.
@en
P2860
P1433
P1476
Probing the active site of Cor ...... d His334-->Gly mutant enzymes.
@en
P2093
Alexandra Schwarz
Lothar Brecker
P2860
P304
P356
10.1111/J.1742-4658.2007.06030.X
P407
P577
2007-09-04T00:00:00Z