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Boolean: (bicycle AND helmet) OR (head AND protection) (always group AND in parenthesis)
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journal:(Journal AND of AND Biological AND Chemistry) AND title:(Tyrosine AND 105 AND and AND threonine AND 212 AND at AND outermost AND substrate AND binding AND subsites AND 6 AND and AND +4 AND control AND substrate AND specificity AND oligosaccharide AND cleavage AND patterns AND and AND multiple AND binding AND modes AND of AND barley AND alpha-amylase AND 1)

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10 items by relevance
1 Journal article

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

Bak-Jensen, Kristian Sass; André, Gwenaëlle; Gottschalk, Tine E; Paës, Gabriel; Tran, Vinh; Svensson, Birte

Journal of Biological Chemistry — 2004, Volume 279, Issue 11, pp. 10093-10102

The role in activity of outer regions in the substrate binding cleft in alpha-amylases is illustrated by mutational analysis of Tyr(105) and Thr(212) localized at subsites -6 and +4 (substrate cleavage occurs between subsites -1 and +1) in barley alpha-amylase 1 (AMY1). Tyr(105) is conserved in plant alpha-amylases whereas Thr(212) varies in these and related enzymes. Compared with wild-type AMY1, the subsite -6 mutant Y105A has 140, 15, and <1% activity (k(cat)/K(m)) on starch, amylose DP17, and 2-chloro-4-nitrophenyl beta-d-maltoheptaoside, whereas T212Y at subsite +4 has 32, 370, and ...

Year: 2004

Language: English

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2 Journal article

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

Bak-Jensen, K.S.; André, G.; Gottschalk, T.E.; Paes, G.; Tran, V.; Svensson, Birte

Journal of Biological Chemistry — 2004, Volume 279, pp. 10093-10102

The role in activity of outer regions in the substrate binding cleft in alpha-amylases is illustrated by mutational analysis of Tyr(105) and Thr(212) localized at subsites - 6 and +4 ( substrate cleavage occurs between subsites -1 and +1) in barley alpha-amylase 1 (AMY1). Tyr(105) is conserved in plant alpha-amylases whereas Thr(212) varies in these and related enzymes. Compared with wild-type AMY1, the subsite -6 mutant Y105A has 140, 15, and <1% activity (k(cat)/K-m) on starch, amylose DP17, and 2-chloro-4-nitrophenyl β-D-maltoheptaoside, whereas T212Y at subsite +4 has 32, 370, and 90...

Year: 2004

Language: English

More...
pgnmakb c h fjiledo

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