Is the enzyme a powerful reactant of the biochemical reaction? (Q28305302)

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English	Is the enzyme a powerful reactant of the biochemical reaction?	scientific article

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instance of

scholarly article

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title

Is the enzyme a powerful reactant of the biochemical reaction? (English)

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author name string

Alexander G Foigel

series ordinal

1

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language of work or name

English

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publication date

June 2011

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published in

Molecular and Cellular Biochemistry

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volume

352

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issue

1-2

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page(s)

87-9

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cites work

Einfluss der Configuration auf die Wirkung der Enzyme

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Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

The Catalytic and Regulatory Properties of Enzymes

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

The depth of chemical time and the power of enzymes as catalysts.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Thermodynamic and extrathermodynamic requirements of enzyme catalysis

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Cooperativity of enzymatic reactions and molecular aspects of energy transduction

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Mechanism of adenosine triphosphate hydrolysis by actomyosin

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Kinetics of Nucleoside Triphosphate Cleavage and Phosphate Release Steps by Associated Rabbit Skeletal Actomyosin, Measured Using a Novel Fluorescent Probe for Phosphate †

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Translational motion of actin filaments in the presence of heavy meromyosin and MgATP as measured by Doppler broadening of laser light scattering

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Ballistic Protons and Microwave-induced Water Solitons in Bioenergetic Transformations

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FS11010-011-0742-4

retrieved

21 January 2018

Computer simulation and analysis of the reaction pathway of triosephosphate isomerase

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/21318350

retrieved

12 December 2020

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Identifiers

DOI

10.1007/S11010-011-0742-4

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Dimensions Publication ID

1018992814

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Fatcat ID

release_sz366sbrbbga7khbzx6bhrjvse

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PubMed publication ID

21318350

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