The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

about

Diversity and regulation of ATP sulfurylase in photosynthetic organisms.Comparative enzymology of the adenosine triphosphate sulphurylases from leaf tissue of selenium-accumulator and non-accumulator plants.Kinetic mechanism of ATP-sulphurylase from rat chondrosarcoma.

P2860

Q34454560-AA45A782-21C1-4BEB-BE50-3019C0DDD401 Q41809065-24517F2D-D90A-4CBC-8E08-A74099F2CDCA Q42827976-1FB114AE-DABB-44C8-A53C-D78D05470034

P2860

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

Item

http://www.wikidata.org/entity/Q41880127

description

1974 nî lūn-bûn

@nan

1974年の論文

@ja

1974年論文

@yue

1974年論文

@zh-hant

1974年論文

@zh-hk

1974年論文

@zh-mo

1974年論文

@zh-tw

1974年论文

@wuu

1974年论文

@zh

1974年论文

@zh-cn

name

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

@en

type

Item

label

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

@en

prefLabel

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

@en

P1476

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

@en

P2093

Anderson JW

http://www.w3.org/2001/XMLSchema#string

Shaw WH

http://www.w3.org/2001/XMLSchema#string

P2860

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory

The isolation of a tryptophan-activating enzyme from pancreas.

Adenosine 5'-sulphatophosphate kinase activity in spinach leaf tissue.

Properties and substrate specificities of the phenylalanyl-transfer-ribonucleic acid synthetases of Aesculus species.

Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue.

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.

On the rate law and mechanism of the adenosine triphosphate--pyrophosphate isotope exchange reaction of amino acyl transfer ribonucleic acid synthetases.

Isoleucyl transfer ribonucleic acid synthetase. The role of magnesium in amino acid activation.

Reactions sequence of leucine activation catalysed by leucyl-RNA synthetase. 1. Kinetic studies.

Standard Gibbs free energy, enthalpy, and entropy changes as a function of pH and pMg for several reactions involving adenosine phosphates.

P304

27-35

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1042/BJ1390027

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

139

http://www.w3.org/2001/XMLSchema#string

P577

1974-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

18701962

http://www.w3.org/2001/XMLSchema#string

P698

4463947

http://www.w3.org/2001/XMLSchema#string

P921

adenosine triphosphate

P932

1166247

http://www.w3.org/2001/XMLSchema#string

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

about

P2860

P2860

The enzymology of adenosine triphosphate sulphurylase from spinach leaf tissue.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932