Properties and Regulation of Aspartate Kinase from Barley Seedlings (Hordeum Vulgare L.)

Overview

Journal Plant Physiol

Specialty Physiology

Date 1977 Jan 1

PMID 16659791

Citations 13

Authors

P R Shewry

B J Miflin

Affiliations

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Abstract

Aspartate kinase (EC 2.7.2.4) has been purified 8-fold and characterized from germinating barley (Hordeum vulgare) seedlings. The enzyme is inhibited 50% by 0.7 mm l-lysine and almost completely at 5 mm. l-Methionine does not affect the enzyme on its own, but at low concentrations (0.1-1 mm) increases the inhibition in the presence of lysine, indicating that the two amino acids act as cooperative feedback regulators.

Citing Articles

Regulation of threonine biosynthesis in barley seedlings (Hordeum vulgare L.).

Aarnes H Planta. 2014; 140(2):185-92.

PMID: 24414476 DOI: 10.1007/BF00384919.

Aspartate kinase and the synthesis of aspartate-derived amino acids in wheat.

Bright S, Shewry P, Miflin B Planta. 2014; 139(2):119-25.

PMID: 24414150 DOI: 10.1007/BF00387136.

The effect of aspartate-derived amino acids (lysine, threonine, methionine) on the growth of excised embryos of wheat and barley.

Bright S, WOOD E, Miflin B Planta. 2014; 139(2):113-7.

PMID: 24414149 DOI: 10.1007/BF00387135.

Studies on lysine analogs, aspartate-derived amino acids, and attempted mutant selection on oat seedlings.

Cummings D, Green C, Stuthman D Planta. 2013; 145(4):309-14.

PMID: 24317756 DOI: 10.1007/BF00388354.

Isolation of a recessive barley mutant resistant to S-(2-aminoethyl)L-cysteine.

Bright S, Norbury P, Miflin B Theor Appl Genet. 2013; 55(1):1-4.

PMID: 24306383 DOI: 10.1007/BF00282969.

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