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Information on EC 3.5.1.1 - asparaginase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38986

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.1 asparaginase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P38986 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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L-asparagine
+
H2O
=
L-aspartate
+
NH3
+
=
+
Synonyms
asparaginase, l-asnase, asrgl1, asparaginase ii, l-asparaginase ii, erwinase, ecaii, l-asparaginase i, ecaiii, diasp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-asparaginase
-
-
-
-
asparaginase II
colaspase
-
-
-
-
crasnitin
-
-
-
-
DiAsp
-
-
-
-
elspar
-
-
-
-
L-ASNase
-
-
-
-
L-asparaginase
-
-
-
-
L-asparaginase-II
-
-
L-asparagine amidohydrolase
-
-
-
-
leunase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-asparagine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9015-68-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Asn + H2O
L-Asp + NH3
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075 - 0.74
L-asparagine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
217 - 523
L-asparagine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13 - 16
L-asparagine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
196.2
-
pH 8.8, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
isoelectric focussing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
L-asparaginase-I is constitutive
Manually annotated by BRENDA team
L-asparaginase-II is secreted in response to N starvation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
high-yield extraction of the periplasmic asparaginase produced by the recombinant Pichia pastoris strain habouring the Saccharomyes cerevisiae ASP3 gene. The use of six freeze-thaw cycles, folllowed by extraction with 20 mM potassium phosphate buffer pH 7.0 for 20 h, resulted in 85% enzyme recovery whereas the alkaline extraction using 500 mM potassium phosphate at pH 11.5 in the presence of 10 mM cysteine allows 100% enzyme recovery
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
178000
gel filtration
400000
-
enzyme I
45000
-
x * 45000, SDS-PAGE, recombinant protein
800000
-
enzyme II
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K215A
-
99.9% loss of activity
T141A
-
99.9% loss of activity
T64A
-
99.9% loss of activity
Y78A
-
99.9% loss of activity
additional information
-
residues T64, Y78, T141, K15 are involved in catalysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the crude asparaginase preparations are stable upon storage at -18°C for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris under the control of the AOX1 gene promoter. High cell density cultures performed with Pichia pastoris harbouring the ASP3 gene using a 2 l instrumented bioreactor, where biomass concentration reached 107 g/l, results in a dramatic increase in volumetric yield (85600 U/l) and global volumetric productivity (1083 U/l)
-
expressed in Pichia pastoris, haboring the ASP3 gene of asparaginase from Saccharomyces cervisiae
-
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wriston, J.C.
Asparaginase
Methods Enzymol.
113
608-618
1985
Azotobacter vinelandii, Acinetobacter calcoaceticus, Klebsiella aerogenes, Saccharomyces cerevisiae, Cavia porcellus, Chlamydomonas sp., Citrobacter freundii, Escherichia coli, Pectobacterium carotovorum, Fusarium tricinctum, Lupinus angustifolius, Lupinus arboreus, Lupinus polyphyllus, Pisum sativum, Proteus vulgaris, Stenotrophomonas geniculata, Serratia marcescens, Wolinella succinogenes
Manually annotated by BRENDA team
Wriston, J.C.; Yellin, T.O.
L-Asparaginase: a review
Adv. Enzymol. Relat. Areas Mol. Biol.
39
185-248
1973
Acinetobacter calcoaceticus, Acinetobacter glutaminasificans, Cupriavidus necator, Aspergillus niger, Aspergillus oryzae, Aspergillus terreus, Azotobacter agilis, Geobacillus stearothermophilus, Clostridium cadaveris, Weizmannia coagulans, Saccharomyces cerevisiae, Brucella abortus, Cavia porcellus, Gallus gallus, Lablab purpureus, Escherichia coli, Erwinia aroidea, Pectobacterium carotovorum, Fusarium tricinctum, Lupinus luteus, Platyrrhini, Mycobacterium tuberculosis, Mycobacterium avium, Mycobacterium tuberculosis variant bovis, Mycolicibacterium phlei, Mycolicibacterium smegmatis, Neurospora crassa, Proteus vulgaris, Pseudomonas sp., [Pseudomonas] boreopolis, Pseudomonas fluorescens, Rattus norvegicus, Salmonella typhosa, Serratia marcescens, Staphylococcus sp., Streptomyces griseus, Escherichia coli EC-I, Pseudomonas sp. P-210, Pseudomonas sp. GG13
Manually annotated by BRENDA team
Verma, N.; Kumar, K.; Kaur, G.; Anand, S.
L-asparaginase: a promising chemotherapeutic agent
Crit. Rev. Biotechnol.
27
45-62
2007
Aliivibrio fischeri, Enterobacter cloacae, Aspergillus niger, Aspergillus tamarii, Aspergillus terreus, Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38986), Cyberlindnera jadinii, Escherichia coli, Erwinia aroidea, Pectobacterium carotovorum, Erwinia sp., Thermus thermophilus, Lupinus angustifolius, Lupinus arboreus, Mycolicibacterium phlei, Nocardia asteroides, Photobacterium leiognathi, Photobacterium phosphoreum, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens, Rhodotorula toruloides, Rhodotorula mucilaginosa, Serratia marcescens, Sphagnum fallax, Staphylococcus sp., Tetrahymena pyriformis, Vibrio harveyi, Erwinia aroidea NRR LB-138, Pseudomonas aeruginosa 50071
Manually annotated by BRENDA team
Ferrara, M.A.; Severino, N.M.; Mansure, J.J.; Martins, A.S.; Oliveira, E.M.; Siani, A.C.; Pereira, N.; Torres, F.A.; Bon, E.P.
Asparaginase production by a recombinant Pichia pastoris strain harbouring Saccharomyces cerevisiae ASP3 gene
Enzyme Microb. Technol.
39
1457-1463
2006
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Ferrara, M.; Severino, N.; Valente, R.; Perales, J.; Bon, E.
High-yield extraction of periplasmic asparaginase produced by recombinant Pichia pastoris harbouring the Saccharomyces cerevisiae ASP3 gene
Enzyme Microb. Technol.
47
71-76
2010
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Lopes, W.; Santos, B.A.F.D.; Sampaio, A.L.F.; Gregorio Alves Fontao, A.P.; Nascimento, H.J.; Jurgilas, P.B.; Torres, F.A.G.; Bon, E.P.D.S.; Almeida, R.V.; Ferrara, M.A.
Expression, purification, and characterization of asparaginase II from Saccharomyces cerevisiae in Escherichia coli
Protein Expr. Purif.
159
21-26
2019
Saccharomyces cerevisiae (P0CZ17), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Costa, I.M.; Schultz, L.; de Araujo Bianchi Pedra, B.; Leite, M.S.; Farsky, S.H.; de Oliveira, M.A.; Pessoa, A.; Monteiro, G.
Recombinant L-asparaginase 1 from Saccharomyces cerevisiae an allosteric enzyme with antineoplastic activity
Sci. Rep.
6
36239
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team