Biosynthesis of neuroactive amino acids by cysteine synthases in Lathyrus latifolius

Ikegami, Fumio; Horiuchi, Seiichi; Kobori, Masuko; Morishige, Itsuko; Murakoshi, Isamu

doi:10.1016/0031-9422(92)80347-h

Cited by 19 publications

(20 citation statements)

References 19 publications

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“…However, L-OUS-synthesizing activity is generally low even in the presence of a high concentration of hydroxyurea. Relative velocities of the enzymes from Allium tuberosum (45), Brassica juncea (42), Citrullus vulgaris (42), Lathyrus latifolius (44), and Leucaena leucocephala (43) for the synthesis of L-OUS are less than 1% of the velocity to synthesize L-cysteine. Exceptionally, although the enzyme from Spinacia oleracea (40) has a high rate of synthesis of L-OUS, it is only approximately 10% of its L-cysteinesynthesizing velocity.…”

Section: Dcsdmentioning

confidence: 94%

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Establishment of anIn Vitrod-Cycloserine-Synthesizing System by UsingO-Ureido-l-Serine Synthase andd-Cycloserine Synthetase Found in the Biosynthetic Pathway

Uda

Matoba

Kumagai

et al. 2013

Antimicrob Agents Chemother

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We have recently cloned a DNA fragment containing a gene cluster that is responsible for the biosynthesis of an antituberculosis antibiotic, D-cycloserine. The gene cluster is composed of 10 open reading frames, designated dcsA to dcsJ. Judging from the sequence similarity between each putative gene product and known proteins, DcsC, which displays high homology to diaminopimelate epimerase, may catalyze the racemization of O-ureidoserine. DcsD is similar to O-acetylserine sulfhydrylase, which generates L-cysteine using O-acetyl-L-serine with sulfide, and therefore, DcsD may be a synthase to generate O-ureido-L-serine using O-acetyl-L-serine and hydroxyurea. DcsG, which exhibits similarity to a family of enzymes with an ATP-grasp fold, may be an ATP-dependent synthetase converting O-ureido-D-serine into D-cycloserine. In the present study, to characterize the enzymatic functions of DcsC, DcsD, and DcsG, each protein was overexpressed in Escherichia coli and purified to near homogeneity. The biochemical function of each of the reactions catalyzed by these three proteins was verified by thin-layer chromatography (TLC), high-performance liquid chromatography (HPLC), and, in some cases, mass spectrometry. The results from this study demonstrate that by using a mixture of the three purified enzymes and the two commercially available substrates O-acetyl-L-serine and hydroxyurea, synthesis of D-cycloserine was successfully attained. These in vitro studies yield the conclusion that DcsD and DcsG are necessary for the syntheses of O-ureido-L-serine and D-cycloserine, respectively. DcsD was also able to catalyze the synthesis of L-cysteine when sulfide was added instead of hydroxyurea. Furthermore, the present study shows that DcsG can also form other cyclic D-amino acid analogs, such as D-homocysteine thiolactone.

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Section: Dcsdmentioning

confidence: 94%

“…The O-acetylserine sulfhydrylase enzymes from plant sources were reported previously to display L-OUS-synthesizing activity (40)(41)(42)(43)(44)(45). However, L-OUS-synthesizing activity is generally low even in the presence of a high concentration of hydroxyurea.…”

Section: Dcsdmentioning

confidence: 99%

Establishment of anIn Vitrod-Cycloserine-Synthesizing System by UsingO-Ureido-l-Serine Synthase andd-Cycloserine Synthetase Found in the Biosynthetic Pathway

Uda

Matoba

Kumagai

et al. 2013

Antimicrob Agents Chemother

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“…Production of isoxazolin-5-one is essential for β-ODAP synthesis and appears linked to the normal metabolic activities of cysteine synthase (CS; also known as either O -acetylserine sulfhydrylase or O -acetylserine(thiol)lyase) and CAS [46,47]. In cysteine biosynthesis, CS catalyzes cysteine formation from O-acetylserine and hydrogen sulfide.…”

Section: β-Odap Biosynthesis In Grass Peamentioning

confidence: 99%

“…The biosynthesis of β-ODAP is connected to the sulfur amino acid biosynthetic pathway (Figure 2) [46,47]. β-ODAP is derived from heterocyclic β-(isoxazolin-5-on-2-yl)alanine, formed by a reaction catalyzed by CAS [47].…”

Section: Biosynthesis Of β-Odap In L Sativus Is Related To Sulfurmentioning

confidence: 99%

β-N-Oxalyl-l-α,β-diaminopropionic Acid (β-ODAP) Content in Lathyrus sativus: The Integration of Nitrogen and Sulfur Metabolism through β-Cyanoalanine Synthase

Liu

Chen

et al. 2017

IJMS

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Grass pea (Lathyrus sativus L.) is an important legume crop grown mainly in South Asia and Sub-Saharan Africa. This underutilized legume can withstand harsh environmental conditions including drought and flooding. During drought-induced famines, this protein-rich legume serves as a food source for poor farmers when other crops fail under harsh environmental conditions; however, its use is limited because of the presence of an endogenous neurotoxic nonprotein amino acid β-N-oxalyl-l-α,β-diaminopropionic acid (β-ODAP). Long-term consumption of Lathyrus and β-ODAP is linked to lathyrism, which is a degenerative motor neuron syndrome. Pharmacological studies indicate that nutritional deficiencies in methionine and cysteine may aggravate the neurotoxicity of β-ODAP. The biosynthetic pathway leading to the production of β-ODAP is poorly understood, but is linked to sulfur metabolism. To date, only a limited number of studies have been conducted in grass pea on the sulfur assimilatory enzymes and how these enzymes regulate the biosynthesis of β-ODAP. Here, we review the current knowledge on the role of sulfur metabolism in grass pea and its contribution to β-ODAP biosynthesis. Unraveling the fundamental steps and regulation of β-ODAP biosynthesis in grass pea will be vital for the development of improved varieties of this underutilized legume.

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“…Being a structural analogue (antagonist) of L-glutamic acid, this amino acid exhibits neuroexcitatory activity and can act as a precursor of 3-aminopropionitrile, L-2,4-diaminobutanoic acid and the neurolathyrogenic 3-(N-oxalyl)-L-2,3-diaminopropionic acid (β-N-oxalyl-L-alanine) in some Vicia and Lathyrus species. L-Quisqualic acid (Figure 18) present in Quisqualis species (Combretaceae) has neuroexcitatory (it is a stimulant of L-glutamic acid receptors) activity and is used as a vermicide in Chinese medicine (Figure 18) (KUO & LAMBEIN 1991;IKEGAMI et al 1992;YIGZAW et al 2001).…”

Section: Substituted Alaninesmentioning

confidence: 99%

Biosynthesis of food constituents: Amino acids: 4. Non-protein amino acids - a review

Velı́šek¹,

Kubec²,

Cejpek³

2006

Czech J. Food Sci.

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This review article gives a brief survey of the principal pathways that lead to the biosynthesis of the most important non-protein amino acids occurring in foods and feeds. These amino acids have been divided into the following groups: 3-amino acids and 4-amino acids, N-substituted amino acids, alicyclic amino acids, hydroxyamino acids, sulfur-containing amino acids, basic amino acids, and taurine.

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Biosynthesis of neuroactive amino acids by cysteine synthases in Lathyrus latifolius

Cited by 19 publications

References 19 publications

Establishment of anIn Vitrod-Cycloserine-Synthesizing System by UsingO-Ureido-l-Serine Synthase andd-Cycloserine Synthetase Found in the Biosynthetic Pathway

Establishment of anIn Vitrod-Cycloserine-Synthesizing System by UsingO-Ureido-l-Serine Synthase andd-Cycloserine Synthetase Found in the Biosynthetic Pathway

β-N-Oxalyl-l-α,β-diaminopropionic Acid (β-ODAP) Content in Lathyrus sativus: The Integration of Nitrogen and Sulfur Metabolism through β-Cyanoalanine Synthase

Biosynthesis of food constituents: Amino acids: 4. Non-protein amino acids - a review

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