Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.
about
Crystal structures and molecular dynamics simulations of thermophilic malate dehydrogenase reveal critical loop motion for co-substrate bindingTetrameric malate dehydrogenase from a thermophilic Bacillus: cloning, sequence and overexpression of the gene encoding the enzyme and isolation and characterization of the recombinant enzyme.
P2860
Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Catalytic-rate improvement of ...... lteration in cofactor binding.
@en
Catalytic-rate improvement of ...... lteration in cofactor binding.
@nl
type
label
Catalytic-rate improvement of ...... lteration in cofactor binding.
@en
Catalytic-rate improvement of ...... lteration in cofactor binding.
@nl
prefLabel
Catalytic-rate improvement of ...... lteration in cofactor binding.
@en
Catalytic-rate improvement of ...... lteration in cofactor binding.
@nl
P2093
P2860
P356
P1433
P1476
Catalytic-rate improvement of ...... lteration in cofactor binding.
@en
P2093
Alldread RM
Atkinson T
Halsall DM
Nicholls DJ
Sundaram TK
P2860
P304
P356
10.1042/BJ3050539
P407
P478
305 ( Pt 2)
P577
1995-01-01T00:00:00Z