An additional substrate binding site in a bacterial phenylalanine hydroxylase
about
A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis.SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase.Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
P2860
An additional substrate binding site in a bacterial phenylalanine hydroxylase
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@ast
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@en
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@nl
type
label
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@ast
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@en
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@nl
prefLabel
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@ast
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@en
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@nl
P2093
P2860
P1476
An additional substrate binding site in a bacterial phenylalanine hydroxylase
@en
P2093
Chittaranjan Das
Isaac R Corn
Judith A Ronau
Julian E Fuchs
Kyle T Wagner
Lake N Paul
Mahdi M Abu-Omar
P2860
P2888
P304
P356
10.1007/S00249-013-0919-8
P577
2013-07-17T00:00:00Z
P5875
P6179
1037979650