Abstract
The uptake of 1-14C-DL-alpha-aminoadipate in resting mycelium of Penicillium chrysogenum Wis 54-1255 and its metabolism during benzylpenicillin formation were studied. The pH optimum for uptake at 25 degrees C was 6.4. Over a range of concentrations from 0.01--1.0 mM, approximately 45% of 1-14C-DL-alpha-aminoadipate was taken up by carbon-starved mycelium. 14CO2 was formed at a low rate, and the total formed amounted to only 1--3% of the 1-14C-DL-alpha-aminoadipate supplied. The intracellular pool of alpha-aminoadipate appears to be expandable, depending on the concentration of alpha-aminoadipate in the medium. The rate of penicillin synthesis depended on the intracellular concentration of alpha-aminoadipate. Penicillin biosynthesis achieved half of the maximum rate at an intracellular concentration of 0.06 nmol alpha-aminoadipate/mg dry cell weight. This low concentration, the result of adding 0.01 mM DL-alpha-aminoadipate to the medium, was sufficient to reverse the inhibition of penicillin biosynthesis caused by 10 mM extracellular L-lysine. Aminoadipate appears to be recycled during penicillin formation. Labeled alpha-ketoadipate was formed from alpha-aminoadipate to the extent of about 25%.
MeSH Terms
2-Aminoadipic Acid/metabolism
Amino Acids, Dicarboxylic/metabolism
Carbon Dioxide/biosynthesis
Cysteine/metabolism
Hydrogen-Ion Concentration
Lysine/metabolism
Penicillin G/biosynthesis
Penicillium/metabolism
Penicillium chrysogenum/metabolism
Valine/metabolism
Chemicals
Amino Acids, Dicarboxylic
Carbon Dioxide
2-Aminoadipic Acid
Valine
Lysine
Cysteine
Penicillin G
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Friedrich C G
Demain A L
References (10)
10 references, click to expand
-
The structure of a peptide, containing alpha-aminoadipic acid, cystine and valine, present in the mycelium of Penicillium chrysogenum.
Biochem J. 1960 Aug;76:357-61
PMID: 13794420
-
Mutants of Saccharomycopsis lipolytica defective in lysine catabolism.
J Bacteriol. 1976 Jan;125(1):48-57
PMID: 1245461
-
Homocitrate synthase as the crucial site of the lysine effect on penicillin biosynthesis.
J Antibiot (Tokyo). 1977 Sep;30(9):760-1
PMID: 411778
-
Biosynthesis of penicillin N and cephalosporin C. Antibiotic production and other features of the metabolism of Cephalosporium sp.
Biochem J. 1967 Jun;103(3):877-90
PMID: 6069166
-
Lysine inhibition of in vivo homocitrate synthesis in Penicillium chrysogenum.
J Gen Microbiol. 1974 May;82(1):143-51
PMID: 4853060
-
Relationship of glutaric acid to the homocitric acid pathway of biosynthesis of lysine in yeast.
J Biol Chem. 1969 Mar 25;244(6):1417-23
PMID: 5773046
-
Use of alpha-aminoadipic acid for the biosynthesis of penicillin N and cephalosporin C by a Cephalosporium sp.
Biochem J. 1967 Jun;103(3):891-901
PMID: 6069167
-
Inhibition of penicillin formation by amino acid analogs.
Arch Biochem Biophys. 1956 Sep;64(1):74-9
PMID: 13363415
-
BIOSYNTHESIS OF DIPICOLINIC ACID AND OF LYSINE IN PENICILLIUM CITREO-VIRIDE.
Biochemistry. 1964 Sep;3:1314-22
PMID: 14229675
-
Biochemistry of penicillin and cephalosporin fermentations.
Lloydia. 1974 Jun;37(2):147-67
PMID: 4211838