(Q47983364)

English

Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity.

scientific article published in January 1999

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scholarly article

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity. (English)

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Peter Macheroux

5

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

author name string

Stehr M

1

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Smau L

2

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Singh M

3

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Seth O

4

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Ghisla S

6

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Diekmann H

7

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

publication date

1 January 1999

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

Biological Chemistry

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

380

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

1

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

47-54

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

Effect of selective cysteine --> alanine replacements on the catalytic functions of lysine: N6-hydroxylase.

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

A workbench for multiple alignment construction and analysis

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

Crystal structure of p-hydroxybenzoate hydroxylase

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

A hydrophobic sequence motif common to N-hydroxylating enzymes

1 reference

https://api.crossref.org/works/10.1515%2FBC.1999.006

21 January 2018

Identifiers

10.1515/BC.1999.006

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/10064136

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