Insights into the interaction of human liver arginase with tightly and weakly bound manganese ions by chemical modification and site-directed mutagenesis studies (Q44078415)

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English	Insights into the interaction of human liver arginase with tightly and weakly bound manganese ions by chemical modification and site-directed mutagenesis studies	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

29 November 2017

Insights into the interaction of human liver arginase with tightly and weakly bound manganese ions by chemical modification and site-directed mutagenesis studies (English)

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Europe PubMed Central

PubMed publication ID

29 November 2017

author name string

María S Orellana

1

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29 November 2017

Vasthi López

2

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Europe PubMed Central

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29 November 2017

Elena Uribe

3

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29 November 2017

Marcia Fuentes

4

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29 November 2017

Mónica Salas

5

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29 November 2017

Nelson Carvajal

6

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29 November 2017

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publication date

1 July 2002

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29 November 2017

Archives of Biochemistry and Biophysics

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29 November 2017

403

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29 November 2017

2

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29 November 2017

155-159

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29 November 2017

pH-sensitive control of arginase by Mn(II) ions at submicromolar concentrations

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Interaction of arginase with metal ions: studies of the enzyme from human liver and comparison with other arginases

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Effect of manganese on the quaternary structure of human liver arginase

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Structure of a unique binuclear manganese cluster in arginase

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Altering the Binuclear Manganese Cluster of Arginase Diminishes Thermostability and Catalytic Function

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Roles of conserved residues in the arginase family

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Manganese-dependent inhibition of human liver arginase by borate

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

L-arginine binding to liver arginase requires proton transfer to gateway residue His141 and coordination of the guanidinium group to the dimanganese(II,II) center

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum

1 reference

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7 January 2021

Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Chemical modification and site-directed mutagenesis of human liver arginase: evidence that the imidazole group of histidine-141 is not involved in substrate binding

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

41 Modification of histidyl residues in proteins by diethylpyrocarbonate

1 reference

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7 January 2021

Identification of histidine residues at the active site of Megalobatrachus japonicus alkaline phosphatase by chemical modification

1 reference

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7 January 2021

Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: possible involvement of a histidine residue in the catalytic process.

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium evidence of essential histidine and lysine groups at the active site

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Molecular basis of hyperargininemia: structure-function consequences of mutations in human liver arginase

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

Mutagenesis of rat liver arginase expressed in Escherichia coli: role of conserved histidines

1 reference

https://api.crossref.org/works/10.1016%2FS0003-9861%2802%2900204-7

7 January 2021

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10.1016/S0003-9861(02)00204-7

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Europe PubMed Central

PubMed publication ID

29 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

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