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LacZ β‐galactosidase: Structure and function of an enzyme of historical and molecular biological importance

Protein science, 2012-12, Vol.21 (12), p.1792-1807

2012

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Gata3 participates in a complex transcriptional feedback network to regulate sympathoadrenal differentiation

Development (Cambridge), 2006-10, Vol.133 (19), p.3871-3881

2006

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Elucidating factors important for monovalent cation selectivity in enzymes: E. coli β-galactosidase as a model

Physical chemistry chemical physics : PCCP, 2015-04, Vol.17 (16), p.10899-10909

2015

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An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a (4)H3 conformation provides insights into the formation, conformation, and stabilization of the transition state

Biochemistry and cell biology, 2015-12, Vol.93 (6), p.531

2015

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β-Galactosidase (Escherichia coli) has a second catalytically important Mg2+ site

Biochemical and biophysical research communications, 2007-01, Vol.352 (2), p.566-570

2007

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Ser-796 of β-galactosidase ( Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop

Archives of biochemistry and biophysics, 2012-01, Vol.517 (2), p.111-122

2012

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Transglucosidic reactions of the Aspergillus niger Family 3 β-glucosidase: Qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH

Archives of biochemistry and biophysics, 2005-04, Vol.436 (2), p.254-264

2005

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Direct and indirect roles of His‐418 in metal binding and in the activity of β‐galactosidase (E. coli)

Protein science, 2009-06, Vol.18 (6), p.1281-1292

2009

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Substitution for Asn460 Cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability

Archives of biochemistry and biophysics, 2012-05, Vol.521 (1-2), p.51-61

2012

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

Biochemistry and cell biology, 2010-10, Vol.88 (5), p.861-869

2010

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Trp-49 of the family 3 β-glucosidase from Aspergillus niger is important for its transglucosidic activity: Creation of novel β-glucosidases with low transglucosidic efficiencies

Archives of biochemistry and biophysics, 2006-11, Vol.455 (2), p.110-118

2006

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Importance of Arg-599 of β-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop

Biochemistry and cell biology, 2010-12, Vol.88 (6), p.969-979

2010

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Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry

The protein journal, 2010-01, Vol.29 (1), p.26

2010

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Trp-262 is a key residue for the hydrolytic and transglucosidic reactivity of the Aspergillus niger family 3 β-glucosidase: Substitution results in enzymes with mainly transglucosidic activity

Archives of biochemistry and biophysics, 2005-12, Vol.444 (1), p.66-75

2005

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

Biochemistry (Easton), 2003-11, Vol.42 (46), p.13505-13511

2003

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Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown

The Protein Journal, 2004-01, Vol.23 (1), p.11-23

2004

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Trp-999 of β-Galactosidase (Escherichia coli) Is a Key Residue for Binding, Catalysis, and Synthesis of Allolactose, the Natural Lac Operon Inducer

Biochemistry (Easton), 2003-02, Vol.42 (6), p.1796-1803

2003

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An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a 4 H 3 conformation provides insights into the formation, conformation, and stabilization of the transition state

Biochemistry and cell biology, 2015-12, Vol.93 (6), p.531-540

2015

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Practical Considerations When Using Temperature to Obtain Rate Constants and Activation Thermodynamics of Enzymes with Two Catalytic Steps: Native and N460T-β-Galactosidase (E. coli) as Examples

The Protein Journal, 2009-02, Vol.28 (2), p.96-103

2009

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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

Biochemistry and cell biology, 2004-04, Vol.82 (2), p.275-284

2004

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β-D-Galactopyranosyl azide

Applied biochemistry and biotechnology, 2003, Vol.104 (2), p.97-104

2003

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Thermal denaturation of .beta.-galactosidase and of two site specific mutants

Biochemistry (Easton), 1990-12, Vol.29 (49), p.11001-11008

1990

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Elucidating factors important for monovalent cation selectivity in enzymes: E. coli β-galactosidase as a modelElectronic supplementary information (ESI) available. See DOI: 10.1039/c4cp04952g

2015-04

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LacZ [beta]-galactosidase: Structure and function of an enzyme of historical and molecular biological importance

Protein science, 2012-12, Vol.21 (12), p.1792

2012

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Beta-D-galactopyranosyl azide: its one-step quantitative synthesis using E461G-beta-galactosidase (Escherichia coli) and a demonstration of its potential as a reagent for molecular biology

Applied biochemistry and biotechnology, 2003-02, Vol.104 (2), p.97-104

2003

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LacZ β‐galactosidase: Structure and function of an enzyme of historical and molecular biological importance

Gata3 participates in a complex transcriptional feedback network to regulate sympathoadrenal differentiation

Elucidating factors important for monovalent cation selectivity in enzymes: E. coli β-galactosidase as a model

An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a (4)H3 conformation provides insights into the formation, conformation, and stabilization of the transition state

β-Galactosidase (Escherichia coli) has a second catalytically important Mg2+ site

Ser-796 of β-galactosidase ( Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop

Transglucosidic reactions of the Aspergillus niger Family 3 β-glucosidase: Qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH

Direct and indirect roles of His‐418 in metal binding and in the activity of β‐galactosidase (E. coli)

Substitution for Asn460 Cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability

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

Trp-49 of the family 3 β-glucosidase from Aspergillus niger is important for its transglucosidic activity: Creation of novel β-glucosidases with low transglucosidic efficiencies

Importance of Arg-599 of β-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop

Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry

Trp-262 is a key residue for the hydrolytic and transglucosidic reactivity of the Aspergillus niger family 3 β-glucosidase: Substitution results in enzymes with mainly transglucosidic activity

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

Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown

Trp-999 of β-Galactosidase (Escherichia coli) Is a Key Residue for Binding, Catalysis, and Synthesis of Allolactose, the Natural Lac Operon Inducer

An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a 4 H 3 conformation provides insights into the formation, conformation, and stabilization of the transition state

Practical Considerations When Using Temperature to Obtain Rate Constants and Activation Thermodynamics of Enzymes with Two Catalytic Steps: Native and N460T-β-Galactosidase (E. coli) as Examples

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

β-D-Galactopyranosyl azide

Thermal denaturation of .beta.-galactosidase and of two site specific mutants

Elucidating factors important for monovalent cation selectivity in enzymes: E. coli β-galactosidase as a modelElectronic supplementary information (ESI) available. See DOI: 10.1039/c4cp04952g

LacZ [beta]-galactosidase: Structure and function of an enzyme of historical and molecular biological importance

Beta-D-galactopyranosyl azide: its one-step quantitative synthesis using E461G-beta-galactosidase (Escherichia coli) and a demonstration of its potential as a reagent for molecular biology

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