Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.5.1.1 (
asparaginase
)
2,695
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The nutritional requirements and culture conditions affecting biosynthesis of
L-asparaginase
in a mutant of Escherichia coli HAP designated strain
A-1
were studied. Asparaginase activity was increased by the addition of L-glutamic acid, L-glutamine, or commercial-grade monosodium glutamate. The rate of enzyme synthesis was dependent on the interaction between the pH of the culture and the amount of oxygen dissolved in the medium. A critical oxygen transfer rate essential for
asparaginase
formation was identified, and a fermentation procedure is described in which enzyme synthesis is controlled by aeration rate. Enhancement of
L-asparaginase
activity by monosodium glutamate was inhibited by the presence of glucose, culture pH, chloramphenicol, and oxygen dissolved in the fermentation medium.
...
PMID:Effect of culture conditions on synthesis of L-asparaginase by Escherichia coli A-1. 1 9
A mating between Escherichia coli 4318 (thi leu Las- Hfr) and E. coli
A-1
(Met- Las+ F-) resulted in the formation of prototrophic recombinants having
L-asparaginase
activities at three distinct levels. The physiology of
L-asparaginase
synthesis in these recombinants is decribed. One class of recombinants produced significantly more
L-asparaginase
than E. coli
A-1
. L-Asparaginase synthesis in the recombinants was inhibited by the presence of dissolved oxygen in the medium and was transiently repressed by the presence of glucose in the same manner as that observed in the parental strains. L-Asparaginase activity was increased by the addition of oxalacetate as well as other members of the tricarboxylic acid cycle.
...
PMID:Physiology of L-asparaginase synthesis in recombinants of Escherichia coli A-1. 2 25
The carboxymethylated
L-asparaginase
from Escherichia coli
A-1
--3 was fragmented with cyanogen bromide and the resulting peptides were isolated by using gel filtration on Sephadex G-50 and column chromatography on DE-52. The amino acid sequences of the 7 cyanogen bromide peptides thus obtained were established completely or partially by further fragmentation with trypsin, chymotrypsin and pepsin, and the Dansyl Edman method. Based on the above results and the complete sequences of the tryptic peptides from the carboxymethylated
L-asparaginase
reported in the previous paper, the whole sequence of the enzyme was established. The reported sequence consists of 321 amino acid residues and its calculated molecular weight is 34 080.
...
PMID:The primary structure of L-asparaginase from Escherichia coli. 676 94
