Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.
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Structural insights into the substrate binding and stereoselectivity of giardia fructose-1,6-bisphosphate aldolaseCrystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanismStructure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolasesStructural Basis for Catalysis of a Tetrameric Class IIa Fructose 1,6-Bisphosphate Aldolase from Mycobacterium tuberculosisExploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolasesModifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution.Directed evolution of aldolases for exploitation in synthetic organic chemistryThe dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase.Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.
P2860
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P2860
Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Identification of arginine 331 ...... aldolase of Escherichia coli.
@en
type
label
Identification of arginine 331 ...... aldolase of Escherichia coli.
@en
prefLabel
Identification of arginine 331 ...... aldolase of Escherichia coli.
@en
P2093
P2860
P356
P1433
P1476
Identification of arginine 331 ...... aldolase of Escherichia coli.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560050119
P577
1996-01-01T00:00:00Z