Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations. (Q54590354)

1 June 2018

title

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

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1 June 2018

main subject

Bradyrhizobium japonicum

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Petrovich RM

1

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Litwin S

series ordinal

2

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Jaffe EK

series ordinal

3

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language of work or name

English

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publication date

1 April 1996

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Journal of Biological Chemistry

published in

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volume

271

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issue

15

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page(s)

8692-8699

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Mechanism of action of 5-aminolaevulinate dehydratase from human erythrocytes

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

Porphobilinogen synthase, the first source of Heme's asymmetry

21 January 2018

1 reference

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Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain

21 January 2018

1 reference

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5-Chloro[1,4-13C]levulinic acid modification of mammalian and bacterial porphobilinogen synthase suggests an active site containing two Zn(II).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

5-Chlorolevulinate modification of porphobilinogen synthase identifies a potential role for the catalytic zinc

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

Investigation of the nature of the two metal-binding sites in 5-aminolaevulinic acid dehydratase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

Spatial proximity and sequence localization of the reactive sulfhydryls of porphobilinogen synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

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.271.15.8692

A Mutant Bradyrhizobium japonicum δ-Aminolevulinic Acid Dehydratase with an Altered Metal Requirement Functions in Situ for Tetrapyrrole Synthesis in Soybean Root Nodules

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

The Phylogenetically Conserved Histidines of Escherichia coli Porphobilinogen Synthase Are Not Required for Catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

5-Aminolaevulinic acid dehydratase: structure, function, and mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

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.271.15.8692

Zinc coordination, function, and structure of zinc enzymes and other proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.15.8692

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.271.15.8692

21 January 2018

Identifiers

DOI

10.1074/JBC.271.15.8692

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1 June 2018

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1 June 2018