Amino Acids and gamma-Glutamyl Derivatives in Seeds of Lunaria annua L. Part II.

Larsen, Peder Olesen; Burmester, Sara; Cederberg, G.; Jensen, R. B.; Pederson, C. Th; Larsen, Erik

doi:10.3891/acta.chem.scand.19-1071

Cited by 18 publications

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“…(6) and therefore widespread in nature (Scheme 4.1) [8]. (R)-b-Aminoisobutyric acid has been found in free form in plants (e.g., in Lunaria annua [26]). It occurs as a constituent in phascolosomine isolated from the worm Phascolon strombi [27] and in some cryptophycins [12,28] [e.g., in cryptophycin 1, which only differs from 3 ( Figure 4.1) by the presence of an (R)-b-Aib residue instead of a b-Ala residue].…”

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confidence: 99%

β‐Amino Acid Biosynthesis

Spiteller

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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confidence: 99%

β‐Amino Acid Biosynthesis

Spiteller

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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“…The incorporation of [14C]DAP into L-lysine in young barley seedlings is consistent with the operation of the DAP pathway in this plant (16). Isolation of aminoadipic acid (14) and saccharopine (17) from some plants have been interpreted as evidence for the occurrence of the alternate six-carbon pathway of lysine biosynthesis in higher plants. In our work to elucidate the lysine pathway in plants, we have partially purified a reversible DAP epimerase from maize (23).…”

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Partial Purification and Characterization of Dihydrodipicolinic Acid Reductase from Maize

Tyagi¹,

Henke²,

Farkas³

1983

Plant Physiol.

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Dihydrodipicolinic acid reductase, an enzyme which catalyzes the pyridine nucleotide-linked reduction of dihydrodipicolinic acid to tetrahydrodipicolinic acid in the biosynthetic pathway leading to L-lysine, has been partially purified from maize (Zea mays cv Pioneer 3145) kernels. The crude maize extract and the partially purified enzyme were assayed for dihydrodipicolinic acid reductase by their ability to restore the capability of crude extracts of a mutant Escherichia coli (CGSC 4549; defective in dihydrodipicolinic acid reductase) to synthesize diaminopimelic acid from aspartic acid and pyruvic acid.

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“…Presumably nitriles will yield carboxylic acids; isothiocyanates the corresponding amines (there is some circumstantial evidence that indeed they do (39)) and thence aldehydes etc. ; and thiocyanates thiols and their derivatives (28).…”

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Glucosinolates

Benn¹

1977

Pure and Applied Chemistry

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The catabolism of glucosinolates is reviewed, with particular attention to the formation of "abnormal" products (thiocyanates, and cyano-epithioalkanes). The biological properties of the glucosinolates and catabolites are briefly surveyed. INTRODUC TI ON Some twenty years have elapsed since Ettlinger and Lundeen proposed .!. as the correct structure for glucosinolate anions. HO~~ OS~N OH bso- HO OHSince passing that milestone there have been major achievements in identifying glucosinolates (the list of which now exceeds 70), andin mapping the biosynthetic pathways at the substrate level. There are recent and authoritative reviews of these advances (1) and I propose to say no more about them here. There has also been a fresh discussion of the value of glucosinolates in plant systematics (2), and that too I shall leave aside. Instead I have chosen to concentrate upon the catabolism of glucosinolates, and their biological properties. GLUCOSINOLATE CATABOLISM"Normal Catabolism'~ When plant tissues containing glucosinolates are crushed there is usually formation of isothiocyanates ("mustard oils") (~) corresponding to the aglucone (~). (Itwas the early recognition of this "normal" catabolism which resulted in the old name "mustard oil glucosides" for the glucosinolates).The isothiocyanate-forming enzymes are known as myrosinases and, after soine controversy, it has been established that their role is to function as thioglucoside glucohydrolases (E. C. 3. 2. 3. 1) remarkably catholic in their acceptance of.!. with a wide va:riety of ltsub-197

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Amino Acids and gamma-Glutamyl Derivatives in Seeds of Lunaria annua L. Part II.

Cited by 18 publications

References 0 publications

β‐Amino Acid Biosynthesis

β‐Amino Acid Biosynthesis

Partial Purification and Characterization of Dihydrodipicolinic Acid Reductase from Maize

Glucosinolates

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