Improved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.

Improved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.

Item
http://www.wikidata.org/entity/Q38343177
Molecular structure and novel DNA binding sites located in loops of flap endonuclease-1 from Pyrococcus horikoshiiThe 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activityCharacteristics of two forms of alpha-amylases and structural implication.Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley alpha-amylase 1.Oligosaccharide binding to barley alpha-amylase 1.Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley alpha-amylase 1.Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity.Mutagenesis of asp-569 of glucosyltransferase I glucansucrase modulates glucan and oligosaccharide synthesis.Aromatic residues located close to the active center are essential for the catalytic reaction of flap endonuclease-1 from hyperthermophilic archaeon Pyrococcus horikoshii.Roles of multiple surface sites, long substrate binding clefts, and carbohydrate binding modules in the action of amylolytic enzymes on polysaccharide substratesInteractions of barley α-amylase isozymes with Ca2 + , substrates and proteinaceous inhibitorsSpecific inhibition of barley α-amylase 2 by barley α-amylase/subtilisin inhibitor depends on charge interactions and can be conferred to isozyme 1 by mutation
P2860

Improved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.

Item
http://www.wikidata.org/entity/Q38343177
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Improved activity and modulate ...... ain of barley alpha-amylase 1.
@en
type
label
Improved activity and modulate ...... ain of barley alpha-amylase 1.
@en
prefLabel
Improved activity and modulate ...... ain of barley alpha-amylase 1.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
P356
P1433
P1476
Improved activity and modulate ...... ain of barley alpha-amylase 1.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921