Catalytic mechanism of human UDP-glucose 6-dehydrogenase: in situ proton NMR studies reveal that the C-5 hydrogen of UDP-glucose is not exchanged with bulk water during the enzymatic reaction.
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Catalytic mechanism of human UDP-glucose 6-dehydrogenase: in situ proton NMR studies reveal that the C-5 hydrogen of UDP-glucose is not exchanged with bulk water during the enzymatic reaction.
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Catalytic mechanism of human U ...... during the enzymatic reaction.
@ast
Catalytic mechanism of human U ...... during the enzymatic reaction.
@en
Catalytic mechanism of human U ...... during the enzymatic reaction.
@nl
type
label
Catalytic mechanism of human U ...... during the enzymatic reaction.
@ast
Catalytic mechanism of human U ...... during the enzymatic reaction.
@en
Catalytic mechanism of human U ...... during the enzymatic reaction.
@nl
prefLabel
Catalytic mechanism of human U ...... during the enzymatic reaction.
@ast
Catalytic mechanism of human U ...... during the enzymatic reaction.
@en
Catalytic mechanism of human U ...... during the enzymatic reaction.
@nl
P2860
P1476
Catalytic mechanism of human U ...... during the enzymatic reaction.
@en
P2093
Lothar Brecker
Thomas Eixelsberger
P2860
P304
P356
10.1016/J.CARRES.2012.03.028
P577
2012-04-02T00:00:00Z