In this section
@article{Fujitani:2006:10.1016/j.phytochem.2006.01.003,
author = {Fujitani, Y and Nakajima, N and Ishihara, K and Oikawa, T and Ito, K and Sugimoto, M},
doi = {10.1016/j.phytochem.2006.01.003},
journal = {Phytochemistry},
pages = {668--674},
title = {Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana.},
url = {http://dx.doi.org/10.1016/j.phytochem.2006.01.003},
volume = {67},
year = {2006}
}
TY - JOUR
AB - A cDNA encoding a homolog of mammalian serine racemase, a unique enzyme in eukaryotes, was isolated from Arabidopsis thaliana and expressed in Escherichia coli cells. The gene product, of which the amino acid residues for binding pyridoxal 5'-phosphate (PLP) are conserved in this as well as mammalian serine racemases, catalyzes not only serine racemization but also dehydration of serine to pyruvate. The enzyme is a homodimer and requires PLP and divalent cations, Ca2+, Mg2+, Mn2+, Fe2+, or Ni2+, at alkaline pH for both activities. The racemization process is highly specific toward L-serine, whereas L-alanine, L-arginine, and L-glutamine were poor substrates. The Vmax/Km values for racemase activity of L- and D-serine are 2.0 and 1.4 nmol/mg/min/mM, respectively, and those values for L- and D-serine on dehydratase activity are 13 and 5.3 nmol/mg/min/mM, i.e. consistent with the theory of racemization reaction and the specificity of dehydration toward L-serine. Hybridization analysis showed that the serine racemase gene was expressed in various organs of A. thaliana.
AU - Fujitani,Y
AU - Nakajima,N
AU - Ishihara,K
AU - Oikawa,T
AU - Ito,K
AU - Sugimoto,M
DO - 10.1016/j.phytochem.2006.01.003
EP - 674
PY - 2006///
SN - 0031-9422
SP - 668
TI - Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana.
T2 - Phytochemistry
UR - http://dx.doi.org/10.1016/j.phytochem.2006.01.003
UR - https://www.ncbi.nlm.nih.gov/pubmed/16483618
VL - 67
ER -
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