scholarly journals Regulation of the acidic amino acid permease of Aspergillus nidulans

1972 ◽  
Vol 127 (3) ◽  
pp. 71P-72P
Author(s):  
J H Robinson ◽  
C Anthony ◽  
W T Drabble
Keyword(s):  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Acidic Amino Acid ◽  
Amino Acid Permease

scholarly journals Regulation of the Acidic Amino-acid Permease of Aspergillus nidulans

1973 ◽  
Vol 79 (1) ◽  
pp. 65-80 ◽  
Author(s):  
J. H. Robinson ◽  
C. Anthony ◽  
W. T. Drabble
Keyword(s):  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Acidic Amino Acid ◽  
Amino Acid Permease

scholarly journals Activity and regulation of an acidic amino acid permease of Aspergillus nidulans

1971 ◽  
Vol 124 (5) ◽  
pp. 75P-75p ◽  
Author(s):  
J H Robinson ◽  
C Anthony ◽  
W T Drabble
Keyword(s):  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Acidic Amino Acid ◽  
Amino Acid Permease

scholarly journals The Acidic Amino-acid Permease of Aspergillus nidulans

1973 ◽  
Vol 79 (1) ◽  
pp. 53-63 ◽  
Author(s):  
J. H. Robinson ◽  
C. Anthony ◽  
W. T. Drabble
Keyword(s):  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Acidic Amino Acid ◽  
Amino Acid Permease

scholarly journals Uptake of the β-Lactam Precursor α-Aminoadipic Acid in Penicillium chrysogenum Is Mediated by the Acidic and the General Amino Acid Permease

2004 ◽  
Vol 70 (8) ◽  
pp. 4775-4783 ◽  
Author(s):  
Hein Trip ◽  
Melchior E. Evers ◽  
Jan A. K. W. Kiel ◽  
Arnold J. M. Driessen
Keyword(s):  
Amino Acid ◽  
Penicillium Chrysogenum ◽  
Acid Uptake ◽  
Penicillin Production ◽  
Acid Transport ◽  
Acidic Amino Acid ◽  
Amino Acid Permease ◽  
Relative Contribution ◽  
Amino Acid Permeases ◽  
General Amino Acid Permease

ABSTRACT External addition of the β-lactam precursor α-aminoadipic acid to the filamentous fungus Penicillium chrysogenum leads to an increased intracellular α-aminoadipic acid concentration and an increase in penicillin production. The exact route for α-aminoadipic acid uptake is not known, although the general amino acid and acidic amino acid permeases have been implicated in this process. Their corresponding genes, PcGAP1 and PcDIP5, of P. chrysogenum were cloned and functionally expressed in a mutant of Saccharomyces cerevisiae (M4276) in which the acidic amino acid and general amino acid permease genes (DIP5 and GAP1, respectively) are disrupted. Transport assays show that both PcGap1 and PcDip5 mediated the uptake of α-aminoadipic acid, although PcGap1 showed a higher affinity for α-aminoadipic acid than PcDip5 (Km values, 230 and 800 μM, respectively). Leucine strongly inhibits α-aminoadipic acid transport via PcGap1 but not via PcDip5. This difference was exploited to estimate the relative contribution of each transport system to the α-aminoadipic acid flux in β-lactam-producing P. chrysogenum. The transport measurements demonstrate that both PcGap1 and PcDip5 contribute to the α-aminoadipic acid flux.

scholarly journals Identification of an Acidic Amino Acid Permease Involved in d-Aspartate Uptake in the Yeast Cryptococcus humicola

2021 ◽  
Vol 9 (1) ◽  
pp. 192
Author(s):  
Daiki Imanishi ◽  
Yoshio Kera ◽  
Shouji Takahashi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Yeast Genome ◽  
Acidic Amino Acid ◽  
Oxidative Deamination ◽  
Amino Acid Permease ◽  
Cryptococcus Humicola ◽  
Growth Defects ◽  
Alkaline Conditions ◽  
The Relationship

d-aspartate oxidase (DDO) catalyzes the oxidative deamination of acidic d-amino acids, and its production is induced by d-Asp in several eukaryotes. The yeast Cryptococcus humicola strain UJ1 produces large amounts of DDO (ChDDO) only in the presence of d-Asp. In this study, we analyzed the relationship between d-Asp uptake by an amino acid permease (Aap) and the inducible expression of ChDDO. We identified two acidic Aap homologs, named “ChAap4 and ChAap5,” in the yeast genome sequence. ChAAP4 deletion resulted in partial growth defects on d-Asp as well as l-Asp, l-Glu, and l-Phe at pH 7, whereas ChAAP5 deletion caused partial growth defects on l-Phe and l-Lys, suggesting that ChAap4 might participate in d-Asp uptake as an acidic Aap. Interestingly, the growth of the Chaap4 strain on d- or l-Asp was completely abolished at pH 10, suggesting that ChAap4 is the only Aap responsible for d- and l-Asp uptake under high alkaline conditions. In addition, ChAAP4 deletion significantly decreased the induction of DDO activity and ChDDO transcription in the presence of d-Asp. This study revealed that d-Asp uptake by ChAap4 might be involved in the induction of ChDDO expression by d-Asp.

scholarly journals The amino acid permease ( AAP ) genes CsAAP2A and SlAAP5A / B are required for oomycete susceptibility in cucumber and tomato

2021 ◽  
Author(s):  
Jeroen A. Berg ◽  
Freddy W. K. Hermans ◽  
Frank Beenders ◽  
Hanieh Abedinpour ◽  
Wim H. Vriezen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Permease

Micellar Catalytic Effects on the Kinetics of the Ionization of Basic Amino Acid and Acidic Amino Acid Studied by the Ultrasonic Absorption Method

Langmuir ◽  
1995 ◽  
Vol 11 (5) ◽  
pp. 1477-1481
Author(s):  
Teruyo Yamashita ◽  
Miyuki Yamasaki ◽  
Takayuki Sano ◽  
Shoji Harada ◽  
Hiroshige Yano
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Ultrasonic Absorption ◽  
Absorption Method ◽  
Acidic Amino Acid ◽  
Kinetics Of ◽  
Catalytic Effects
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