Leucine synthesis in spinach chloroplasts: partial characterization of 2-isopropylmalate synthase

P Hagelstein; G Schultz

doi:10.1515/bchm3.1993.374.7-12.1105

Leucine synthesis in spinach chloroplasts: partial characterization of 2-isopropylmalate synthase

Biol Chem Hoppe Seyler. 1993 Dec;374(12):1105-8. doi: 10.1515/bchm3.1993.374.7-12.1105.

Authors

P Hagelstein¹, G Schultz

Affiliation

¹ Botanisches Institut, Tierärztlichen Hochschule Hannover, Germany.

PMID: 8129855
DOI: 10.1515/bchm3.1993.374.7-12.1105

Abstract

Leucine synthesis was found to be localized in chloroplasts of higher plants. The introductory enzyme of the isopropylmalate pathway, the 2-isopropylmalate synthase, was strongly feedback-regulated by leucine. The pH optimum of the enzyme was between 7.0 and 9.0. The Km values were 5 microM for acetyl-CoA and 75 microM for 2-oxoisovalerate.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

2-Isopropylmalate Synthase / metabolism*
Chloroplasts / enzymology
Chloroplasts / metabolism*
Hydrogen-Ion Concentration
Leucine / biosynthesis*
Plants / enzymology
Plants / metabolism*

Substances

2-Isopropylmalate Synthase
Leucine