A highly conserved arginine residue of the chitosanase from Streptomyces sp. N174 is involved both in catalysis and substrate binding
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Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to PhenotypesStructural insights into the substrate-binding mechanism for a novel chitosanaseA highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp. TS Is Involved in the Substrate Binding.Diversity of family GH46 chitosanases in Kitasatospora setae KM-6054.
P2860
A highly conserved arginine residue of the chitosanase from Streptomyces sp. N174 is involved both in catalysis and substrate binding
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2013 nî lūn-bûn
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2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2013年の論文
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2013年論文
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2013年論文
@zh-hant
2013年論文
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2013年論文
@zh-mo
2013年論文
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2013年论文
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A highly conserved arginine re ...... atalysis and substrate binding
@ast
A highly conserved arginine re ...... atalysis and substrate binding
@en
A highly conserved arginine re ...... atalysis and substrate binding
@nl
type
label
A highly conserved arginine re ...... atalysis and substrate binding
@ast
A highly conserved arginine re ...... atalysis and substrate binding
@en
A highly conserved arginine re ...... atalysis and substrate binding
@nl
prefLabel
A highly conserved arginine re ...... atalysis and substrate binding
@ast
A highly conserved arginine re ...... atalysis and substrate binding
@en
A highly conserved arginine re ...... atalysis and substrate binding
@nl
P2093
P2860
P356
P1433
P1476
A highly conserved arginine re ...... atalysis and substrate binding
@en
P2093
Marie-Ève Lacombe-Harvey
Mélanie Fortin
Takayuki Ohnuma
Tamo Fukamizo
Thomas Letzel
P2860
P356
10.1186/1471-2091-14-23
P577
2013-09-16T00:00:00Z