Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions.
about
Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coliStructure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartateThree-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibitionPositive selection of Kranz and non-Kranz C4 phosphoenolpyruvate carboxylase amino acids in Suaedoideae (Chenopodiaceae).The replacement of Lys620 by serine desensitizes Escherichia coli phosphoenolpyruvate carboxylase to the effects of the feedback inhibitors L-aspartate and L-malate.
P2860
Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions.
description
1995 nî lūn-bûn
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1995年の論文
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年學術文章
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1995年學術文章
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1995年學術文章
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name
Site-directed mutagenesis of L ...... ytic and regulatory functions.
@en
type
label
Site-directed mutagenesis of L ...... ytic and regulatory functions.
@en
prefLabel
Site-directed mutagenesis of L ...... ytic and regulatory functions.
@en
P2860
P1433
P1476
Site-directed mutagenesis of L ...... ytic and regulatory functions.
@en
P2860
P356
10.1016/0014-5793(95)01189-L
P407
P577
1995-11-01T00:00:00Z