Information on EC 1.97.1.9 - selenate reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
1.97.1.9
-
RECOMMENDED NAME
GeneOntology No.
selenate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors
-
-
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
electron transport mechanism
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
active site molybdenum
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
selenate transport mechanism
-
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
active site molybdenum
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Selenocompound metabolism
-
SYSTEMATIC NAME
IUBMB Comments
selenite:reduced acceptor oxidoreductase
The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
selenate reductase
-
-
selenate reductase
Enterobacter cloacae SLD1a-1
-
;
-
selenate reductase
-
-
selenate reductase
-
-
selenate reductase
Pseudomonas sp. CA5
-
-
-
selenate reductase
-
-
additional information
-
enzyme probably belongs to the DMSO reductase family of mononuclear molybdenum enzymes
additional information
-
enzyme probably belongs to the DMSO reductase family of mononuclear molybdenum enzymes
-
CAS REGISTRY NUMBER
COMMENTARY
146359-71-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacillus arseniciselenatis
-
-
-
Manually annotated by BRENDA team
subunit SrdA
UniProt
Manually annotated by BRENDA team
subunit SrdB
UniProt
Manually annotated by BRENDA team
subunit SrdC
UniProt
Manually annotated by BRENDA team
ATCC 700258
-
-
Manually annotated by BRENDA team
strain SLD1a-1
-
-
Manually annotated by BRENDA team
strain SLD1a-1, expression under aerobic conditions, poor expression during anaerobic growth on nitrate
-
-
Manually annotated by BRENDA team
strain SLD1a-1; strain SLD1a-1, ATCC 700258, highest activity when molybdate is added to the culture medium
-
-
Manually annotated by BRENDA team
strain SLDa-1
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
-
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
ATCC 700258
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
strain SLD1a-1
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
strain SLD1a-1, expression under aerobic conditions, poor expression during anaerobic growth on nitrate
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
strain SLD1a-1; strain SLD1a-1, ATCC 700258, highest activity when molybdate is added to the culture medium
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLDa-1
strain SLDa-1
-
-
Manually annotated by BRENDA team
genes ygfK, ygfM, and ygfN encode the 3 subunit polypeptides YgfK, YgfM, and YgfN; strain K-12 and derivatives
-
-
Manually annotated by BRENDA team
strain CA5
-
-
Manually annotated by BRENDA team
Pseudomonas sp. CA5
strain CA5
-
-
Manually annotated by BRENDA team
-
Q9S1H0 and Q9S1G9 and Q9S1G7
UniProt
Manually annotated by BRENDA team
selenate-respiring bacterium
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-, E9RFC9, E9RFD0, E9RFD1
expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype; expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype; expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype
physiological function
-
expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype; expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype; expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
selenate + acetate
selenite + H2O + CO2
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Bacillus arseniciselenatis
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
specific for selenate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
specific for selenate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
enzyme also reduces nitrate, thiosulfate, and fumarate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Thauera selenatis, Sulfurospirillum barnesii, Bacillus arseniciselenatis
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
enzyme also reduces nitrate, thiosulfate, and fumarate, selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized donor
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + glucose
?
show the reaction diagram
-
-
-
-
?
selenate + H2
selenite + H2O
show the reaction diagram
-
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
Sulfurospirillum barnesii, Bacillus arseniciselenatis
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
-
-
-
?
selenate + malate
?
show the reaction diagram
Bacillus arseniciselenatis
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
detoxification of selenate
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae SLDa-1
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
-
best electron donor
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + benzyl viologen
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
-
-
-
?
selenate + reduced cytc-Ts4
selenite + H2O + oxidized cytc-Ts4
show the reaction diagram
-
a c-type cytochrom is purified and shown to donate electrons to SerABC in vitro. Redox potentiometry, combined with UV-visible spectroscopy, show that cytc-Ts4 is a diheme cytochrome with a redox potential of +/-282 mV, and both hemes are predicted to have His-Met ligation
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
preferred electron donor
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
11% of the activity with benzyl viologen
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
Enterobacter cloacae SLD1a-1
-
preferred electron donor
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + methyl viologen
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
NADH, succinate, and lactate are no electron donors, no activity with nitrate, nitrite, sulfate, and chlorate
-
-
-
additional information
?
-
-
no activity with nitrate, nitrite, sulfate, and chlorate
-
-
-
additional information
?
-
-
also active on nitrate, thiosulfate and fumarate
-
-
-
additional information
?
-
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
no substrate: nitrate, sulfate, perchlorate, thiosulfate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Thauera selenatis, Sulfurospirillum barnesii, Bacillus arseniciselenatis
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
Q9S1H0 and Q9S1G9 and Q9S1G7
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + H2
selenite + H2O
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae SLD1a-1
-
detoxification of selenate
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
Enterobacter cloacae SLDa-1
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cytochrome b
-
1 cytochrome b per alphabetagamma-trimer
-
cytochrome b
-
-
-
cytochrome b
-
-
-
heme
-
0.9 mol per mol of enzyme
iron-sulfur centre
-
at least 2 [Fe-S]-centre as prosthetic groups per enzyme molecule
molybdopterin
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Iron
-
12.9 mol per mol of enzyme, based on MW 159000; part of at least 2 iron-sulfur centres per enzyme molecule and of the heme group of cytochrome b
Iron
-
in FeS-centres
Iron
-
iron-sulfur centre
Iron
-
non-heme iron, 18 mol per mol of enzyme
Iron
-
[3Fe4S]1+ and [4Fe4S]1+ centres
Molybdenum
-
1 molybdenum per mol of trimer
Molybdenum
-
in the active site
Molybdenum
-
-
Molybdenum
-
enhances the activity 10fold in vivo when added to the growth medium; required
Molybdenum
-
present at the active site
Molybdenum
-
Mo-S, Mo=O and Mo-O bound to enzyme
Molybdenum
-
0.6 mol per mol of enzyme
Molybdenum
-
type II molybdoenzyme
Molybdenum
-
-
Non-heme iron
-
-
selenium
-
isolated enzyme contains a reduced form of selenium, probably as selenocysteine
sulfur
-
iron-sulfur centre
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
selenate
-
mixed-type inhibition
Thiocyanate
-
mixed-type inhibition
tungstate
-
highly inhibitory
tungstate
-
in vitro and in vivo
tungstate
-
SER isolated from periplasmic fractions from cells grown on 1 mM tungstate display selenate reductase activities with a 20fold reduction in Vmax and a 23fold increase in substrate binding affinity. The thermo-stability and pH dependence of tungsten-SER is shown to be similar to that observed for molybdenum-SER
additional information
-
no inhibition by nitrate
-
additional information
-
no inhibition by sodium azide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
selenate
-
induction of enzyme activity when included in growth medium
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.25
-
benzyl viologen
-
20C
0.0007
-
selenate
-
tungsten-SER, pH and temperature not specified in the publication, Vmax: 0.01 micromol/min/mg
0.016
-
selenate
-
pH 6.0
0.016
-
selenate
-
-
0.016
-
selenate
-
molybdenum-SER, pH and temperature not specified in the publication, Vmax: 0.2 micromol/min/mg
2
-
selenate
-
using electron donormethyl viologen
2.1
-
selenate
-
pH 7.2, 30C, holenzyme complex
5.5
-
selenate
-
pH 7.2, 30C, isolated alpha subunit
6.25
-
selenate
-
with reduced benzyl viologen, 20C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5
-
selenate
-
using electron donormethyl viologen
387
-
selenate
-
pH 6.0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
Thiocyanate
-
30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.29
-
-
membrane fraction
0.42
-
Q9S1H0 and Q9S1G9 and Q9S1G7
wild-type
0.76
-
-
wild-type, cells grown on nitrate
1.6
-
-
wild-type, cells grown on selenate + nitrate
3.84
-
-
wild-type, cells grown on selenate
41.4
-
-
purified enzyme
500
-
-
pH 7.2, 30C
additional information
-
-
activity in nirate reductase deficient mutants under different growth conditions
additional information
-
-
microtiter plate assay method based on enzyme-dependent reoxidation of reduced methyl viologen detected at 600 nm. Assay is fast and allows for simultaneous testing of a range of alternative substrates and multiple samples
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
65
-
-
optimal temperature for molybdenum-SER
80
-
-
optimal temperature for tungsten-SER is higher than 80C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Bacillus arseniciselenatis
-
maximal growth at a pH range of pH 9.0-11.0
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
with localisation of the catalytic site to the periplasmic side of the membrane
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1
-
with localisation of the catalytic site to the periplasmic side of the membrane
-
-
Manually annotated by BRENDA team
-
loosely associated with the cytoplasmic membrane
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1, Enterobacter cloacae SLDa-1
-
-
-
-
Manually annotated by BRENDA team
Enterobacter cloacae SLD1a-1, Enterobacter cloacae SLDa-1, Sulfurospirillum barnesii SES-3
-
-
-
Manually annotated by BRENDA team
additional information
-
not in the cytosol
-
Manually annotated by BRENDA team
additional information
Enterobacter cloacae SLD1a-1
-
not in the cytosol
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
160000
-
-
-
180000
-
-
gel filtration
180000
-
-
-
600000
-
-
gel filtration
700000
-
-
native gel electrophoresis of cell-free extracts and activity stain
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nonamer
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
nonamer
Enterobacter cloacae SLD1a-1
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
-
tetramer
-
1 * 82000 + 1 * 53000 + 1 *34000 + 1* 21000
tetramer
-
alphabetagammadelta, 1 * 82000 + 1 * 53000 + 1 * 34000 + 1 * 21000
tetramer
-
1 * 82000 + 1 * 53000 + 1 *34000 + 1* 21000
-
trimer
-
1 * 96000, alpha, + 1 * 40000, beta, + 1 * 23000, gamma, SDS-PAGE
trimer
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
trimer
-
alphabetagamma, 1 * 96000 + 1 * 40000 + 1 * 23000
trimer
-
alpha, beta, gamma
trimer
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
additional information
-
1 cytochrome b per alphabetagamma-complex
additional information
-
the gamma subunit may be identical with the cytochrome b
additional information
-
heterotrimeric complex: apparent about 600000 Da (3 alpha-subunits + 3 beta-subunits + 3 gamma-subunits), alpha-subunit: about 100000 Da, beta-subunit: about 55000 Da, gamma-subunit: about 36000 Da
additional information
Enterobacter cloacae SLD1a-1
-
heterotrimeric complex: apparent about 600000 Da (3 alpha-subunits + 3 beta-subunits + 3 gamma-subunits), alpha-subunit: about 100000 Da, beta-subunit: about 55000 Da, gamma-subunit: about 36000 Da
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapour diffusion method, precipitation by ammonium sulfate, protein solution: 10 mg/ml, 0.3-0.5 M ammonium sulfate, 50 mM piperazine, pH 6.0, reservoir solution: 1.8-2.2 M ammonium sulfate, 100 mM Tris-HCl, pH 8.0-8.9, 293 K, 2-4 weeks, cryoprotection by 25% glycerol, X-ray structure determination and analysis
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
purified molybdenum-SER complex is stable and active upon heat-shock incubation for 10 min at temperatures up to 60C. At temperatures greater than 65C all three subunits (SerABC) are readily denatured
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, enzyme extracted with Thesit retains 50% activity after being frozen for prolonged periods
-
4C, enzyme extracted with Thesit remains active for 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
57fold, to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
-, E9RFC9, E9RFD0, E9RFD1
DNA sequence determination and analysis, contruction of gene bank, genomic organisationand potential function of: genes serA, serB, and serC, additional overlapping serD
Q9S1H0 and Q9S1G9 and Q9S1G7
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
construction of diverse Tn5 insertion mutants by transposon mutagenesis, overview
additional information
Q9S1H0 and Q9S1G9 and Q9S1G7
construction of Tn5 insertion mutants by transposon mutagenesis using Escherichia coli strain S17-1 as partner, loss of activity