Information on EC 1.8.99.2 - adenylyl-sulfate reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.8.99.2
-
RECOMMENDED NAME
GeneOntology No.
adenylyl-sulfate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
sulfate reduction
-
-
sulfate reduction IV (dissimilatory)
-
-
sulfate reduction V (dissimilatory)
-
-
sulfite oxidation II
-
-
sulfite oxidation III
-
-
Sulfur metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming)
An iron flavoprotein (FAD). Methyl viologen can act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-75-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain D
-
-
Manually annotated by BRENDA team
Columbia ecotype
-
-
Manually annotated by BRENDA team
archaebacterium
VC-16
-
-
Manually annotated by BRENDA team
archaebacterium VC-16
VC-16
-
-
Manually annotated by BRENDA team
subunit A and subunit B
O28603 and O28604
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Astragalus tephrosioides
-
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
DBO1
-
-
Manually annotated by BRENDA team
DBO1
-
-
Manually annotated by BRENDA team
genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain CM, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain CM, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain TLS, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain CaD3, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain CaD3, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain BS1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain BS1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
Chromatium sp.
weak activity
-
-
Manually annotated by BRENDA team
strain MLMS-1
-
-
Manually annotated by BRENDA team
strain MLMS-1
-
-
Manually annotated by BRENDA team
strain MI-1
-
-
Manually annotated by BRENDA team
strain MI-1
-
-
Manually annotated by BRENDA team
strain DSM 12254
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Marburg
-
-
Manually annotated by BRENDA team
strain Miyazaki
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki F
alpha subunit and beta subunit; strain Miyazaki F
B8PS61 and B8DS74
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
weak activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BU-1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
f. sp. thiosulfatophilum
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
beta-subunit
UniProt
Manually annotated by BRENDA team
Tetraselmis sp.
-
-
-
Manually annotated by BRENDA team
large subunit AprA and small subunit AprB
F6KEW4 and F6KEW3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
APS reductase is a key enzyme involved in the pathways of sulfate reduction and sulfide oxidation in the biological sulfur cycle
physiological function
-
key enzyme of the dissimilatory sulfate respiration
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-adenylylsulfate + dithioerythritol
adenosine 5'-monophosphate + sulfite + oxidized dithioerythritol
show the reaction diagram
-
-
-
-
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
show the reaction diagram
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
adenylyl sulfate + dithioerythritol
AMP + sulfite + ?
show the reaction diagram
adenylyl sulfate + dithioerythritol
AMP + sulfite + oxidized dithioerythritol
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithionite
AMP + sulfite + ?
show the reaction diagram
adenylyl sulfate + dithiothreitol
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + ferrocytochrome c3
AMP + sulfite + ferricytochrome
show the reaction diagram
adenylyl sulfate + GSH
AMP + sulfite + GSSG
show the reaction diagram
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
adenylyl sulfate + reduced glutaredoxin 1
AMP + sulfite + oxidized glutaredoxin 1
show the reaction diagram
-
can use 3'-phosphoadenylyl sulfate as sulfate donor
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
adenylyl sulfate + reduced thioredoxin
AMP + sulfite + oxidized thioredoxin
show the reaction diagram
adenylyl sulfate + reduced thioredoxin 1
AMP + sulfite + oxidized thioredoxin 1
show the reaction diagram
adenylylsulfate + thioredoxin
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
ADP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
AMP + sulfite + acceptor
adenylyl sulfate + reduced acceptor
show the reaction diagram
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
show the reaction diagram
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
AMP + sulfite + [Fe(CN)6]3-
adenylyl sulfate + [Fe(CN)6]4-
show the reaction diagram
F6KEW4 and F6KEW3
-
-
-
-
ATP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
CMP + sulfite + cytochrome c
cytidylyl sulfate + ?
show the reaction diagram
-
7% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
dAMP + sulfite + cytochrome c
deoxyadenylyl sulfate + ?
show the reaction diagram
-
80% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
show the reaction diagram
GMP + sulfite + cytochrome c
guanylyl sulfate + ?
show the reaction diagram
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
guanylyl sulfate + reduced methyl viologen
GMP + methyl viologen + sulfite
show the reaction diagram
-
-
-
-
?
IMP + sulfite + cytochrome c
?
show the reaction diagram
-
62% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
UMP + sulfite + cytochrome c
uridylyl sulfate + ?
show the reaction diagram
-
9% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
dihydroriboflavin
-
can donate electrons directly to adenylyl sulfate reductase
FADH2
-
can donate electrons directly to adenylyl sulfate reductase
flavin
FMNH2
-
can donate electrons directly to adenylyl sulfate reductase
heme
-
contains 2 heme groups of cytochrome c characterper mol of enzyme
iron-sulfur centre
-
two [4Fe-4S] clusters are enveloped by cluster-binding motifs
additional information
-
the enzyme contains a [4Fe-4S] cluster cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S cluster
flavoenzyme.The two electrons required for adenylyl sulfate reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD. The large difference in reduction potential of these clusters (-60 mV and -500 mV) can be explained by interactions of the clusters with the protein matrix
Fe2+
-
the enzyme contains a [4Fe-4S] cluster cofactor
Iron-sulfur cluster
iron-sulfur clusters
-
iron-sulfur flavoprotein containing two distinct [4Fe-4S] dusters
additional information
-
stimulation by high ionic strength
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[2-(1,2-dicarboxyethylamino)ethylamino]butanedioic acid
O28603 and O28604
-
-
2-[2-[bis(carboxymethyl)amino]ethyl-(2-hydroxymethyl)amino]acetic acid
O28603 and O28604
-
-
3'-phosphoadenosine-5'-phosphate
-
-
cysteine
-
1 mM, significant inhibition
EDTA
O28603 and O28604
-
iodoacetamide
NaN3
-
10 mM, no loss of the activity with ferricyanide, 52% loss of the activity with cytochrome c
potassium phosphate
-
inhibits reaction with cytochrome c
Sodium arsenite
-
10 mM, no loss of the activity with ferricyanide, 88% loss of the activity with cytochrome c
additional information
-
inhibitor binding structure, binding energies, dissociation constants, and inhibition mechanisms, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
buthionine sulfoximine
-
1 mM, 2fold stimulation of activity
menadione
-
stimulates oxidation of ferrocytochrome c3 with adenylyl sulfate and FAD as electron mediator
Na2SO4
NaCl
-
APR activity of all three isoforms increases 3fold in roots after 5 h of treatment with 150 mM NaCl
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
5'-adenylylsulfate
-
-
0.0065 - 0.25
adenylyl sulfate
0.0025 - 1
AMP
3.1
CMP
-
reaction with cytochrome c
0.021 - 0.033
cytochrome c
0.0002
dithiothreitol
-
-
0.089 - 4.2
ferricyanide
0.022
glutaredoxin 1
-
pH 8 and saturating adenylyl sulfate
-
0.01 - 3
GMP
0.025
guanylyl sulfate
-
-
0.8 - 1.5
IMP
0.015
riboflavin
-
-
0.017 - 2.5
sulfite
2.7 - 8.6
thioredoxin
0.053
thioredoxin 1
-
pH 8 and saturating adenylyl sulfate
4.5
UMP
-
reaction with cytochrome c
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Desulfovibrio desulfuricans
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0003
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0005
0.0006
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0013
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0017
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.011
mutant enzyme 342S
0.15
mutant enzyme 345S
0.302
-
mutant enzyme C140S, at 30C in 100 mM Tris-HCl buffer pH 8.0 containing 1 mM EDTA, 5 mM DTT, 0.106 mM thioredoxin from Escherichia coli, and 0.05 mM APS
2.39
archaebacterium
-
-
3.5
mutant enzyme C250S
4.6
-
untagged APS reductase using Escherichia coli thioredoxin
5.1
-
His-tagged APS reductase using Escherichia coli thioredoxin
7.248
wild type enzyme
10.3
-
wild type enzyme, at 30C in 100 mM Tris-HCl buffer pH 8.0 containing 1 mM EDTA, 5 mM DTT, 0.106 mM thioredoxin from Escherichia coli, and 0.05 mM APS
30 - 40
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
oxidation of methyl viologen
7
-
ferricyanide assay, phosphate buffer
7.7
-
reaction with ferricyanide
8.5
-
reaction with adenylyl sulfate and dithiothreitol
8.8
-
reaction with cytochrome c
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
archaebacterium
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 90
archaebacterium
-
70C: about 65% of maximal activity, 90C: about 90% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
axenic cell suspension culture
Manually annotated by BRENDA team
-
APS reductase enhances strongly in the shoots of sulfate-deprived plants, and rapidly decreases again upon sulfate re-supply
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
exclusively located in chloroplast
Manually annotated by BRENDA team
additional information
-
mitochondrial or cytoplasmic localization
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
calculated from sequence of cDNA, C-terminal domain of EiAPR; MALDI-TOF mass spectrometry, C-terminal domain of EiAPR
28350
-
calculated average mass, determined on the elemental composition of the apoprotein plus the components in the metal center, assuming that all cysteines are in reduced form and the metal cluster has an oxidation state of zero
28360
-
calculated from amino acid sequence
28560
-
calculated from amino acid sequence
28700
-
gel filtration
30470
-
MALDI-TOF mass spectrometry, the enzyme used is a recombinant protein with 48 additional residues containing the His6 tag
35000
-
SDS-PAGE
35430
-
mass spectrometry
48000
non-reducing and reducing SDS-PAGE
48700
-
MALDI-TOF mass spectrometry, whole enzyme
48710
-
calculated from sequence of cDNA, whole enzyme
52000
-
SDS-PAGE
90000 - 124000
-
dynamic light scattering
96000
non-reducing SDS-PAGE, 16% of the protein was present as a homodimer
160000
170000
175000
180000
186000
-
smallest catalytic active subunit, also aggregations of 324000 Da and 569000 Da are detected, gel filtration
190000
-
gel filtration
200000
-
estimation from sedimentation coefficient
210000
-
gel filtration
400000
-
gel filtration
439500
-
equilibrium sedimentation
600000
-
gel filtration, the majority of the protein is aggregated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterohexamer
-
non-functional protein
heterotetramer
-
1 * 75000 + 1 * 20000, alpha2beta2 heterotetramer
hexamer
-
APSR comprises six alphabeta-heterodimers that form a hexameric structure, X-ray crystallography
homodimer
monomer
oligomer
Q59339 and Q59338
2 * 80000 + 1 * 18500, alpha2beta structure, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; the structures of the enzyme in the two-electron reduced state and with sulfite bound to FAD are reported at 1.6 A and 2.5 A resolution, respectively
hanging-drop vapour-diffusion method using PEG 4000 as precipitant. Crystals grow in space group P2(1)2(1)2(1), with unit-cell parameters a = 72.4, b = 113.2, c = 194.0 A. The asymmetric unit probably contains two units. The crystals diffract beyond 2 A resolution and are suitable for X-ray structure analysis
O28603 and O28604
dynamic light scattering, ultracentrifugation, and electron paramagnetic resonance methods
-
hanging drop vapor diffusion method, using 20% (w/v) PEG 6000 and 60 mM ammonium sulfate in Tris buffer (0.1 M, pH 7.0), at 18C
-
hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 0.1 M NaCl, 2.0 M ammonium sulfate and 15% (v/v) glycerol, at 4C
B8PS61 and B8DS74
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
2 h, more than 30% loss of activity
65
-
5 min, complete loss of activity
70
-
2 min, 50% loss of activity
75
-
thermotolerant up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
30-50% loss of activity by repeated freezing and thawing
-
enzyme is rapidly denatured by even micromolar concentrations of ferricyanide
-
total enzyme activity is significantly decreased by ammonium sulfate precipitation, leaving 20% of the initial activity in the supernatant
F6KEW4 and F6KEW3
unstable to air with a half-life of 12 min, the 4Fe-4S cluster is converted into a 2Fe-2S form
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen causes complete loss of activity
-
659441
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 88-90% loss of activity after 1 week, 68% loss of activity after 16 days, in presence of 50% glycerol, 46% loss of activity after 16 days
-
-20C, much loss of activity after 30 days
-
-20C, stable for several weeks
-
4C, continous loss of activity
-
4C, continous loss of activity, precipitation after 2-3 days
-
4C, more than 2 days, more than 30% loss of activity
-
4C, more than 20% loss of activity after 8 h
-
5C, 5 days, 20% loss of activity
-
frozen, protein concentration above 5 mg/ml, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DE-52 column chromatography, macro-DEAE column chromatography, and hydroxyapatite column chromatography
-
DEAE-Biogel A chromatography, Source 15 column chromatography, and Superdex 200 column chromatography
-
DEAE-Toyopearl 650S column chromatography, Sephacryl S-200 gel filtration, and Superdex 200 gel filtration
B8PS61 and B8DS74
HiTrap chelating column chromatography
-
isolated under the exclusion of oxygen
O28603 and O28604
Ni2+ affinity chromatography
Ni2+-affinity column chromatography
-
partial purification by ammonium sulfate precipitation and Q-Sepharose column chromatography
F6KEW4 and F6KEW3
purification of a recombinant His-tagged protein and several mutants by Ni2+ affinity chromatography
-
purification of a recombinant tagged protein by chitin affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Eschericha coli as the N-terminal reductase domain (AcAPR1-N) and the C-terminal glutaredoxin domain (AcAPR1-C). Recombinant full-length ATP sulfurylase (AcATPS1) and recombinant full length adenosine-5'-phosphosulfate reductase (AcAPR1) from Allium cepa can form a physical association
-
expressed in Escherichia coli
expressed in Escherichia coli JM109 cells
-
expressed in Zea mays
-
expression in Escherichia coli
-
expression in Escherichia coli of a recombinant His-tagged protein and several mutants
-
expression in Escherichia coli of a tagged recombinant protein
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation; full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
gene apsA, PCR-based DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
localized expression in plastids of Arabidopsis thaliana, transgenic plants accumulate sulfite, thiosulfate, cysteine and gluthatione
-
overexpression in Escherichia coli
overexpression of a His-tagged recombinant protein in Escherichia coli
-