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L-Asparaginase Of Saccharomyces Cerevisiae: An Extracellular Enzyme.

P. C. Dunlop, R. Roon
Published 1975 · Biology, Medicine

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During recent studies conducted with suspensions of three strains of Saccharomyces cerevisiae, it was observed that ammonia was rapidly liberated when L-asparagine was added to the medium. Subsequent investigation has revealed that these strains of S. cerevisiae have an externally active asparaginase as well as an internally active one. The appearance of the external asparaginase is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The internal enzyme appears to be constitutive. The external activity is relatively insensitive to para-hydroxymercuribenzoate inhibition, whereas the internal activity is highly inhibited by this compound.



This paper is referenced by
10.1111/j.1567-1364.2012.00828.x
The ASP3 locus in Saccharomyces cerevisiae originated by horizontal gene transfer from Wickerhamomyces.
Garrett P. League (2012)
10.1099/00221287-131-9-2253
Saccharomyces cerevisiae to Mutants Resistant -L-Aspartylhydroxamate
G. Jones (1985)
Screening of Microbial Isolates for the Fermentative Production of L-Asparaginase in Submerged Fermentation
K. Balakrishnan (2013)
Detecting, Modelling, and Interpreting Gene-by-Environment Interactions
Emily S Nelson (2017)
10.1007/BF02920425
Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme.
E. P. Bon (1997)
L-Asparaginase from Microbes: a Comprehensive Review
D. S. Kumar (2012)
10.1021/BI00596A008
Possible site-specific reagent for the general amino acid transport system of Saccharomyces cerevisiae.
F. Larimore (1978)
10.1128/JB.147.1.9-12.1981
Regulation of L-asparaginase in a Chlamydomonas species in response to ambient concentrations of combined nitrogen.
J. Paul (1981)
10.1002/JCTB.4121
Performance improvement of Bacillus aryabhattai ITBHU02 for high-throughput production of a tumor-inhibitory L-asparaginase using a kinetic model based approach
Y. Singh (2014)
10.1111/J.1432-1033.1979.TB12908.X
Synthesis and activation of asparagine in asparagine auxotrophs of Saccharomyces cerevisiae.
F. Ramos (1979)
10.1104/PP.68.6.1364
Regulation of asparaginase, glutamine synthetase, and glutamate dehydrogenase in response to medium nitrogen concentrations in a euryhaline chlamydomonas species.
J. Paul (1981)
10.3389/fbioe.2019.00016
Fed-Batch Production of Saccharomyces cerevisiae L-Asparaginase II by Recombinant Pichia pastoris MUTs Strain
David Rodrigues (2019)
10.1177/1082013209353219
Effect of Medium Composition and Kinetic Studies on Extracellular and Intracellular Production of L-asparaginase from Pectobacterium carotovorum
S. Arrivukkarasan (2010)
10.1099/00221287-95-2-391
The relationship between methionine uptake and demethiolation in a methionine-utilizing mutant of Pseudomonas fluorescens UK1.
S. Laakso (1976)
SHORT COMMUNICATION Asparaginase 11 of Saccharomyces cerevisiae : Characterization of a Mutation that Affects Expression in Rapidly Growing Cells
K. D. Pauling (1980)
10.1080/10826068.2020.1815053
Glutaminase-free L-asparaginase production by Leucosporidium muscorum isolated from Antarctic marine-sediment.
R. K. B. Freire (2020)
10.1016/J.IFSET.2020.102397
Effect of innovative pre-treatments on the mitigation of acrylamide formation in potato chips
Maria Alessia Schouten (2020)
10.1099/00221287-117-2-423
Asparaginase II of Saccharomyces cerevisiae: Dynamics of Accumulation and Loss in Rapidly Growing Cells
K. D. Pauling (1980)
10.1007/BF00335825
Factors affecting l-asparaginase activity in soils
W. Frankenberger (2004)
Utilization of-Asparagine bySaccharomyces cerevisiae
R. Roon (1976)
10.1016/0005-2744(80)90144-8
Asparaginase II of Saccharomyces cerevisiae: inactivation during the transition to stationary phase.
K. D. Pauling (1980)
10.1016/0003-9861(82)90138-2
Derepression of asparaginase II during exponential growth of Saccharomyces cerevisiae on ammonium ion.
R. Roon (1982)
10.1016/j.pep.2019.02.012
Expression, purification, and characterization of asparaginase II from Saccharomyces cerevisiae in Escherichia coli.
Wagner Lopes (2019)
10.1099/00221287-119-2-539
Asparaginase II of Saccharomyces cerevisiae: Characterization of a Mutation that Affects Expression in Rapidly Growing Cells
K. D. Pauling (1980)
10.1111/J.1567-1364.2007.00252.X
Single QTL mapping and nucleotide-level resolution of a physiologic trait in wine Saccharomyces cerevisiae strains.
P. Marullo (2007)
Asparaginase II ofSaccharomyces cerevisiae: Positive Selection of TwoMutations ThatPrevent EnzymeSynthesis
K. W. Kim (1984)
10.1016/B978-0-444-63662-1.00012-9
Therapeutic Enzymes: l-Asparaginases
J. Vidya (2017)
10.1016/J.AB.2006.09.024
Enzymatic assay of allantoin in serum using allantoinase and allantoate amidohydrolase.
H. Muratsubaki (2006)
Production, Purification & Characterization of Extracellular L-Asparaginase (Anti Cancerous Enzyme) From Aspergillus niger
Kuldeep Luhana (2013)
10.1007/978-1-4612-2312-2_19
Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme.
E. P. Bon (1997)
10.1016/j.biortech.2010.07.114
Purification and characterization of glutaminase-free L-asparaginase from Pectobacterium carotovorum MTCC 1428.
S. Kumar (2011)
10.1371/journal.pone.0154722
Genome Sequencing and Comparative Analysis of Saccharomyces cerevisiae Strains of the Peterhof Genetic Collection
P. Drozdova (2016)
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