Pig heart fumarase contains two distinct substrate-binding sites differing in affinity (Q77580809)

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6 December 2019

title

Pig heart fumarase contains two distinct substrate-binding sites differing in affinity (English)

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6 December 2019

author name string

S Beeckmans

series ordinal

1

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6 December 2019

E Van Driessche

series ordinal

2

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6 December 2019

language of work or name

English

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publication date

1 November 1998

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Journal of Biological Chemistry

6 December 2019

published in

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6 December 2019

volume

273

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6 December 2019

issue

48

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6 December 2019

page(s)

31661-31669

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Evidence that rat liver mitochondrial and cytosolic fumarases are synthesized from one species of mRNA by alternative translational initiation at two in-phase AUG codons.

6 December 2019

cites work

1 reference

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The multisubunit active site of fumarase C from Escherichia coli

21 January 2018

1 reference

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Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli

21 January 2018

1 reference

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Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.

21 January 2018

1 reference

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Use of isotope effects to deduce the chemical mechanism of fumarase.

21 January 2018

1 reference

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Chicken heart fumarase: its purification and physico-chemical characterization. A comparison with the enzyme from pig heart

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

The modification with tetranitromethane of an essential tyrosine in the active site of pig fumarase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Lack of deviation from Michaelis--Menten kinetics for pig heart fumarase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Pig heart fumarase really does exhibit negative kinetic co-operativity at a constant ionic strength

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Proton transfer in catalysis by fumarase

21 January 2018

1 reference

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Role of conformational change in the fumarase reaction cycle.

21 January 2018

1 reference

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Restructuring the active site of fumarase for the fumarate to malate reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

A new purification procedure for fumarase based of affinity chromatography. Isolation and characterization of pig-liver fumarase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

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Purification and crystallization of fumarase C from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Amino acid sequence of porcine heart fumarase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Subunit interactions in pig heart fumarase--I. Study of tetramer-dimer equilibrium in dilute urea solutions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Immobilized enzymes as tools for the demonstration of metabolon formation. A short overview

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Physiological significance of metabolic channelling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12.

21 January 2018

1 reference

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L-Aspartate-induced activation of aspartase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Kinetic studies of L-aspartase from Escherichia coli: substrate activation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Activation of aspartase by site-directed mutagenesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

Characterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.48.31661

21 January 2018

Identifiers

DOI

10.1074/JBC.273.48.31661

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9822627%20AND%20SRC:MED&resulttype=core&format=json

6 December 2019

1 reference