Biosynthesis of lysine in plants: Evidence for a variant of the known bacterial pathways

TY - JOUR

T1 - Biosynthesis of lysine in plants

T2 - Evidence for a variant of the known bacterial pathways

AU - Hudson, Andre O.

AU - Bless, Christine

AU - MacEdo, Polliana

AU - Chatterjee, Siba P.

AU - Singh, Bijay K.

AU - Gilvarg, Charles

AU - Leustek, Thomas

N1 - Funding Information: This work is dedicated to the memory of Prof. S.P. Chatterjee (deceased 2000). The work was supported by a grant from the American Cyanamid Company (C.G.), the National Science Foundation grant IBN-9817594 (T.L.). Andre’ Hudson was supported by a training grant GM55145 funded by the National Institutes of Health and is currently the recipient of a National Institutes of Health Predoctoral Fellowship GM069264. Prof. S.P. Chatterjee, Department of Botany Burdwan University, Burdwan, India, was recipient of a Fulbright Travel Grant, Council of International Exchange of Scholars, USA. Christine Bless and Polliana Macedo contributed to the work as undergraduate students enrolled in the Biology and Biotechnology Curriculum, respectively, at the Cook College division of Rutgers University.

PY - 2005/1/19

Y1 - 2005/1/19

N2 - With the aim of elucidating how plants synthesize lysine, extracts prepared from corn, tobacco, Chlamydomonas and soybean were tested and found to lack detectable amounts of N-α-acyl-l,l-diaminopimelate deacylase or N-succinyl-α-amino-ε-ketopimelate-glutamate aminotransaminase, two key enzymes in the central part of the bacterial pathway for lysine biosynthesis. Corn extracts missing two key enzymes still carried out the overall synthesis of lysine when provided with dihydrodipicolinate. An analysis of available plant DNA sequences was performed to test the veracity of the negative biochemical findings. Orthologs of dihydrodipicolinate reductase and diaminopimelate epimerase (enzymes on each side of the central pathway) were readily found in the Arabidopsis thaliana genome. Orthologs of the known enzymes needed to convert tetrahydrodipicolinate to diaminopimelic acid (DAP) were not detected in Arabidopsis or in the plant DNA sequence databases. The biochemical and reinforcing bioinformatics results provide evidence that plants may use a novel variant of the bacterial pathways for lysine biosynthesis.

AB - With the aim of elucidating how plants synthesize lysine, extracts prepared from corn, tobacco, Chlamydomonas and soybean were tested and found to lack detectable amounts of N-α-acyl-l,l-diaminopimelate deacylase or N-succinyl-α-amino-ε-ketopimelate-glutamate aminotransaminase, two key enzymes in the central part of the bacterial pathway for lysine biosynthesis. Corn extracts missing two key enzymes still carried out the overall synthesis of lysine when provided with dihydrodipicolinate. An analysis of available plant DNA sequences was performed to test the veracity of the negative biochemical findings. Orthologs of dihydrodipicolinate reductase and diaminopimelate epimerase (enzymes on each side of the central pathway) were readily found in the Arabidopsis thaliana genome. Orthologs of the known enzymes needed to convert tetrahydrodipicolinate to diaminopimelic acid (DAP) were not detected in Arabidopsis or in the plant DNA sequence databases. The biochemical and reinforcing bioinformatics results provide evidence that plants may use a novel variant of the bacterial pathways for lysine biosynthesis.

KW - Amino acid metabolism

KW - Arabidopsis thaliana

KW - Diaminopimelate

KW - Dihydrodipicolinate

KW - Lysine

KW - Plant

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U2 - https://doi.org/10.1016/j.bbagen.2004.09.008

DO - https://doi.org/10.1016/j.bbagen.2004.09.008

M3 - Article

C2 - 15652176

SN - 0006-3002

VL - 1721

SP - 27

EP - 36

JO - BBA - Biochimica et Biophysica Acta

JF - BBA - Biochimica et Biophysica Acta

IS - 1-3

ER -