scholarly journals Nitrogenous compounds and nitrogen metabolism in the Liliaceae. 4. Isolation of azetidine-2-carboxylic acid and evidence for the occurrence of αγ-diaminobutyric acid in Polygonatum*

1958 ◽  
Vol 70 (4) ◽  
pp. 626-629 ◽  
Author(s):  
L. Fowden ◽  
Mary Bryant
1968 ◽  
Vol 46 (7) ◽  
pp. 909-919 ◽  
Author(s):  
D. J. Durzan

Buds, shoot apices, and leaves from terminal shoots of white spruce saplings accumulated high levels of alcohol-soluble nitrogen in spring, late summer, and early winter. Major components, e.g. arginine, glutamine and proline, of the soluble nitrogen showed patterns complementary to each other. These changes represented the storage and mobilization of nitrogenous compounds during the onset of dormancy or the growth of shoots. Leaves contained less total soluble nitrogen than buds or shoot apices. Soluble nitrogen and arginine content of leaves resembled buds in their seasonal patterns but changes in aspartic acid, glutamic acid, and alanine were much greater than in buds, especially in late summer.When the first frost appeared, uniformly labelled 14C-arginine, applied to the apices of buds, readily entered newly synthesized protein, and free arginine was converted to proline via ornithine. Proline with carbon derived from arginine also entered proteins that were metabolized at different rates. A fraction of the proline in protein was hydroxylated to hydroxyproline. Although traces of 14C-citrulline were detected, more carbon was metabolized to free guanidino compounds, e.g. α-keto-δ-guanidinovaleric acid, γ-guanidinobutyric acid, and several monosubstituted guanidines. After 24 hours, labelled arginine, proline, and γ-guanidinobutyric acid moved down the shoot to the leaves. These metabolic changes in buds show that many of the seasonal changes in amino acids are intimately related to the carbon and nitrogen metabolism of arginine.


1991 ◽  
Vol 46 (7-8) ◽  
pp. 527-533 ◽  
Author(s):  
K. Taraz ◽  
R. Tappe ◽  
H. Schröder ◽  
U. Hohlneicher ◽  
I. Gwose ◽  
...  

Abstract From ferribactins which accompany pyoverdins in iron deficient cultures of fluorescent pseudomonads a subunit has been obtained formed by condensation of D-tyrosin with L-2,4-diaminobutyric acid to give 2-(1-R-amino-2-p-hydroxyphenylethyl)-1,4,5,6-tetrahydropyrimidine-4-S′-carboxylic acid (1). Evidence is presented that 1 is the precur or of the typical pyoverdin chromophore 7 a.


1957 ◽  
Vol 21 (2) ◽  
pp. 193-201 ◽  
Author(s):  
R. M. ZACHARIUS ◽  
H. M. CATHEY ◽  
F. C. STEWARD

1992 ◽  
Vol 47 (7-8) ◽  
pp. 487-502 ◽  
Author(s):  
I. Gwose ◽  
K. Taraz

The structures of two pyoverdins (Pp 1 and Pp 2) and one dihydropyoverdin (dihydro-Pp 2) from a strain of Pseudomonas putida have been elucidated by spectroscopic methods and degradation studies. The pyoverdins Pp 1 and Pp2 consist of a chromophore which was identified as (1 S)-5-amino-2,3-dihydro-8,9-dihydroxy-1 H-pyrimido[1,2-a]quinoline-1-carboxylic acid substituted at the amino group with a 3-carboxypropanoyl or a succinamoyl residue and at the carboxy group with the N-terminus of L-Ser-L-Thr-D-Ser-L-Orn-L-threo-(OH)Asp-[D-Gln + L-Dab]*-L-Ser-D-allo-Thr-L-c(OH)Orn. Dihydro-Pp 2 differs from Pp 2 only in the chromophore, which is saturated at carbons 5 and 6. All compounds contain a tetrahydropyrimidine moiety ([D-Gln + L-Dab]*) resulting from the condensation of 2,4-diaminobutyric acid and glutamine.


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