@article{ref1,
title="Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana",
journal="Biochemical journal",
year="1994",
author="Jones, R. M. and Jordan, P. M.",
volume="299 ( Pt 3)",
number="Pt 3",
pages="895-902",
abstract="Porphobilinogen deaminase (EC 4.3.1.8) has been purified to homogeneity (16,000-fold) from the plant Arabidopsis thaliana in yields of 8%. The deaminase is a monomer of M(r) 35,000, as shown by SDS/PAGE, and 31,000, using gel-filtration chromatography. The pure enzyme has a Vmax. of 4.5 mumol/h per mg and a Km of 17 +/- 4 microM. Determination of the pI and pH optimum revealed values of 5.2 and 8.0 respectively. The sequence of the N-terminus was found to be NH2-XVAVEQKTRTAI. The deaminase is heat-stable up to 70 degrees C and is inhibited by NH3 and hydroxylamine. The enzyme is inactivated by arginine-, histidine- and lysine-specific reagents. Incubation with the substrate analogue and suicide inhibitor, 2-bromoporphobilinogen, results in chain termination and in inactivation.<p /><p>Language: en</p>",
language="en",
issn="0264-6021",
doi="10.1042/bj2990895",
url="http://dx.doi.org/10.1042/bj2990895"
}