scholarly journals Conversion of Tyrosine Phenol-lyase to Dicarboxylic Amino Acid β-Lyase, an Enzyme Not Found in Nature

1999 ◽  
Vol 274 (3) ◽  
pp. 1320-1325 ◽  
Author(s):  
Barbara Mouratou ◽  
Patrik Kasper ◽  
Heinz Gehring ◽  
Philipp Christen
Keyword(s):  
Amino Acid ◽  
Dicarboxylic Amino Acid ◽  
Tyrosine Phenol Lyase

scholarly journals Dicarboxylic Amino Acid Uptake in Normal, Friedreich's Ataxia, and Dicarboxylic Aminoaciduria Fibroblasts

1979 ◽  
Vol 6 (2) ◽  
pp. 263-273 ◽  
Author(s):  
S.B. Melancon ◽  
B. Grenier ◽  
L. Dallaire ◽  
M. Potier ◽  
G. Fontaine ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Uptake ◽  
Friedreich’S Ataxia ◽  
Friedreich's Ataxia ◽  
Acid Uptake ◽  
Normal Cells ◽  
Dicarboxylic Amino Acid ◽  
Normal Individuals ◽  
Kinetics Of

SummaryGlutamic and aspartic acid uptake was measured in skin fibroblasts from patients with Friedreich's Ataxia, dicarboxylic aminoaciduria, and normal individuals. The results showed no difference in uptake kinetics of either dicarboxylic amino acids between Friedreich's Ataxia and normal cells, but reduced uptake velocities in dicarboxylic aminoaciduria fibroblasts. Friedreich's Ataxia fibroblasts were, however, less calcium-dependant and more magnesium and phosphate-dependent than controls in glucose-free incubation mixture. This difference might be related to some degree of glucose intolerance by Friedreich's Ataxia fibroblasts in culture.

scholarly journals AgtA, the Dicarboxylic Amino Acid Transporter of Aspergillus nidulans, Is Concertedly Down-Regulated by Exquisite Sensitivity to Nitrogen Metabolite Repression and Ammonium-Elicited Endocytosis

2009 ◽  
Vol 8 (3) ◽  
pp. 339-352 ◽  
Author(s):  
Angeliki Apostolaki ◽  
Zoi Erpapazoglou ◽  
Laura Harispe ◽  
Maria Billini ◽  
Panagiota Kafasla ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Amino Acid Transporter ◽  
Acid Transport ◽  
Transport Activity ◽  
High Affinity ◽  
Nitrogen Metabolite Repression ◽  
Dicarboxylic Amino Acid ◽  
Specific Induction ◽  
Acid Transporter

ABSTRACT We identified agtA, a gene that encodes the specific dicarboxylic amino acid transporter of Aspergillus nidulans. The deletion of the gene resulted in loss of utilization of aspartate as a nitrogen source and of aspartate uptake, while not completely abolishing glutamate utilization. Kinetic constants showed that AgtA is a high-affinity dicarboxylic amino acid transporter and are in agreement with those determined for a cognate transporter activity identified previously. The gene is extremely sensitive to nitrogen metabolite repression, depends on AreA for its expression, and is seemingly independent from specific induction. We showed that the localization of AgtA in the plasma membrane necessitates the ShrA protein and that an active process elicited by ammonium results in internalization and targeting of AgtA to the vacuole, followed by degradation. Thus, nitrogen metabolite repression and ammonium-promoted vacuolar degradation act in concert to downregulate dicarboxylic amino acid transport activity.

scholarly journals Evidence for essential histidine and dicarboxylic amino-acid residues in the active site of UDP-glucose : solasodine glucosyltransferase from eggplant leaves.

2003 ◽  
Vol 50 (2) ◽  
pp. 567-572 ◽  
Author(s):  
Paulina Nawłoka ◽  
Małgorzata Kalinowska ◽  
Cezary Paczkowski ◽  
Zdzisław A Wojciechowski
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Active Site ◽  
Inhibitory Effect ◽  
Amino Acid Residues ◽  
Chemical Probes ◽  
Dicarboxylic Amino Acid ◽  
Enzyme Substrates ◽  
Arginine Residues

Effects of several chemical probes selectively modifying various amino-acid residues on the activity of UDP-glucose : solasodine glucosyltransferase from eggplant leaves was studied. It was shown that diethylpyrocarbonate (DEPC), a specific modifier of histidine residues, was strongly inhibitory. However, in the presence of excessive amounts of the enzyme substrates, i.e. either UDP-glucose or solasodine, the inhibitory effect of DEPC was much weaker indicating that histidine (or histidines) are present in the active site of the enzyme. Our results suggest also that unmodified residues of glutamic (or aspartic) acid, lysine, cysteine, tyrosine and tryptophan are necessary for full activity of the enzyme. Reagents modifying serine and arginine residues have no effect on the enzyme activity.

Genetic incorporation ofl-dihydroxyphenylalanine (DOPA) biosynthesized by a tyrosine phenol-lyase

2018 ◽  
Vol 54 (24) ◽  
pp. 3002-3005 ◽  
Author(s):  
Sanggil Kim ◽  
Bong Hyun Sung ◽  
Sun Chang Kim ◽  
Hyun Soo Lee
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Tyrosine Phenol Lyase ◽  
Genetic Incorporation

l-Dihydroxyphenylalanine (DOPA) was biosynthesized by a tyrosine-phenol lyase from catechol, pyruvate, and ammonia inEscherichia coli, and the biosynthesized amino acid was directly incorporated into proteins.

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