(Q42677110)

4 November 2017

title

Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites (English)

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4 November 2017

Tarun AS

1

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4 November 2017

Theologis A

series ordinal

2

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4 November 2017

language of work or name

English

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publication date

1 May 1998

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Journal of Biological Chemistry

4 November 2017

published in

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4 November 2017

volume

273

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4 November 2017

issue

20

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4 November 2017

page(s)

12509-12514

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Ethylene biosynthesis: Identification of 1-aminocyclopropane-1-carboxylic acid as an intermediate in the conversion of methionine to ethylene

4 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Stereochemical course of the reaction catalyzed by the pyridoxal phosphate-dependent enzyme 1-aminocyclopropane-1-carboxylate synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

1-Aminocyclopropane-1-carboxylate synthase in tomato is encoded by a multigene family whose transcription is induced during fruit and floral senescence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in zucchini (Cucurbita pepo) are clustered and similar but differentially regulated

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Aminotransferases: demonstration of homology and division into evolutionary subgroups.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Use of monoclonal antibodies in the purification and characterization of 1-aminocyclopropane-1-carboxylate synthase, an enzyme in ethylene biosynthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Characterization and sequencing of the active site of 1-aminocyclopropane-1-carboxylate synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: protein complementation reveals shared active sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

DNA sequencing with chain-terminating inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Formation of functional cross-species heterodimers of ornithine decarboxylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

Co-operativity in seminal ribonuclease function. Kinetic studies

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.273.20.12509

21 January 2018

Identifiers

DOI

10.1074/JBC.273.20.12509

1 reference

4 November 2017

1 reference