Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli) (Q27664904)

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English	Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli)	scientific article

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instance of

scholarly article

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title

Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli) (English)

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main subject

Escherichia coli

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author name string

Megan L Dugdale

series ordinal

1

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Dayna L Dymianiw

series ordinal

2

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Bhawanjot K Minhas

series ordinal

3

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Igor D'Angelo

series ordinal

4

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Reuben E Huber

series ordinal

5

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publication date

October 2010

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published in

Biochemistry and Cell Biology

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volume

88

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issue

5

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page(s)

861-9

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cites work

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Expression and nucleotide sequence of the Clostridium acetobutylicum beta-galactosidase gene cloned in Escherichia coli

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Effects of various concentrations of Na+ and Mg2+ on the activity of β-galactosidase

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21 January 2018

Strong inhibitory effect of furanoses and sugar lactones on beta-galactosidase Escherichia coli.

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A quantitation of the factors which affect the hydrolase and transgalactosylase activities of β-galactosidase (E. coli) on lactose

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21 January 2018

Interaction of divalent cations with .beta.-galactosidase (Escherichia coli)

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Genetic regulatory mechanisms in the synthesis of proteins

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Three-dimensional structure of beta-galactosidase from E. coli

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lac Repressor-operator interaction. VI. The natural inducer of the lac operon.

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21 January 2018

High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for α-complementation

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A structural view of the action of Escherichia coli (lacZ) beta-galactosidase

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Structural Basis for the Altered Activity of Gly794 Variants of Escherichia coli β-Galactosidase†

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Two genes encoding the beta-galactosidase of Lactobacillus sake

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Sequence of the Kluyveromyces lactis beta-galactosidase: comparison with prokaryotic enzymes and secondary structure analysis

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Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences

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A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase.

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Substitutions for Glu-537 of beta-galactosidase from Escherichia coli cause large decreases in catalytic activity

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retrieved

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Identifiers

DOI

10.1139/O10-009

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PubMed publication ID

20921997

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