(Q27638453)

6

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author name string

Eileen K Jaffe

1

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Jukka Kervinen

2

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Jacob Martins

3

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Frederic Stauffer

4

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Reinhard Neier

5

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Alexander Zdanov

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

31 May 2002

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published in

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volume

277

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issue

22

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page(s)

19792-9

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cites work

The porphobilinogen synthase family of metalloenzymes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

An artificial gene for human porphobilinogen synthase allows comparison of an allelic variation implicated in susceptibility to lead poisoning

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

The molecular mechanism of lead inhibition of human porphobilinogen synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Improved methods for building protein models in electron density maps and the location of errors in these models

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Mobile unnatural amino acid side chains in the core of staphylococcal nuclease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Characterization of the two 5-aminolaevulinic acid binding sites, the A- and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Porphobilinogen synthase, the first source of Heme's asymmetry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

Observation of covalent intermediates in an enzyme mechanism at atomic resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201486200

release_paty4yme7fg5zccnvmcjqwfrbq

21 January 2018

Identifiers

DOI

10.1074/JBC.M201486200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/paty4yme7fg5zccnvmcjqwfrbq