Information on EC 2.8.1.1 - thiosulfate sulfurtransferase

-

NEM

-

Ni2+

-

more than 70% inhibition at 0.1 mM

oxaloacetate

-

645511

p-chloromercuribenzoate

Phenylglyoxal

-

pyruvate

-

S-nitroso-glutathione

-

dithiothreitol prevents enzyme inhibition and fully restores enzyme activity

645521

S-nitroso-N-acetyl-penicillamine

-

dithithreitol prevents enzyme inhibition and fully restores enzyme activity

645521

SDS

-

SO32-

19 entries

SO42-

-

incubation of mitochondria with sulfate causes a significant decrease in activity

sodium arsenite

-

Sodium borohydride

-

pH 8.0

succinate

-

sulfhydryl reagents

-

Sulfide

-

activating at 0.1 mM, inhibitory above 0.3 mM, in human colon cancer cell line HT-29

sulfite

thiocyanate

-

thiosulfate

Triton X-100

-

slight

Zn2+

2-mercaptoethanol

4-carbamothioylphenyl 2-(acetyloxy)benzoate

P24329

i.e. H2S-releasing aspirin, ATB-340. Pretreatment by H2S donors NaHS and 4-carbamothioylphenyl 2-(acetyloxy)benzoate in aged rats reduces the oxidative index levels and correlate with thiosulfate-dithiol sulfurtransferase activity

761166

Butyrate

-

significantly increase of enzyme activity and expression in human colon cancer cell line HT-29

671241

dihydrolipoate

-

increases activity at low concentrations

dithioerythritol

-

maximal activation at 0.005 mM, inhibition above

glutathione

-

increases activity at low concentrations

L-cysteine

reduced glutathione

-

enhances activity

Sulfide

-

activating at 0.1 mM, inhibitory above 0.3 mM, in human colon cancer cell line HT-29

671241

sulfite

-

activating effect at high thiosulfate concentrations in p-dimethylaminoazobenzene-treated mice

645539

3.7 - 51.7

3-Mercaptopyruvate

0.03 - 27

CN-

19 entries

0.27 - 14

cyanide

6 entries

8.8

H2S

-

20°C, pH 9.2

0.05

Polysulfide

-

pH 9.0, 80°C

-

6.9

tetrathionate

-

pH 9.0, 80°C

0.017 - 0.034

thioredoxin

0.53 - 603

thiosulfate

46 entries

0.7 - 54

3-Mercaptopyruvate

0.52

cyanide

Q8NFU3

37°C, pH 7.4

761486

2.8 - 400

thiosulfate

6 entries

1.94

cyanide

37°C, pH 7.4

0.003

-

intestine

0.008

-

abomasum

0.01

0.012

-

enzyme from muscle, pH 9.2, 37°C

0.014

-

intestine

0.015

-

with H2S as substrate

0.016

-

omasum

0.017

-

spleen

0.018

-

rumen

0.02

0.026

-

abomasum

0.027

0.029

-

rumen

0.03

Equus caballus

-

enzyme from lung, pH 9.2, 37°C

0.033

-

rumen

0.035

-

enzyme from brain, pH 9.2, 37°C

0.04

0.046

0.047

-

oesophagus

0.05

0.06

0.069

-

rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of methionine

0.07

0.071

0.077

-

rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of cysteine

0.078

-

rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiocystine

0.08

0.085

-

rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-4-carboxylic acid

0.09

0.092

-

kidney

0.1

-

microsomal rhodanese 28 days after common bile duct ligation

0.11

-

rhodanese activity in muscle of omasum of male and female animals

0.113

-

rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-2,4-dicarboxylic acid

0.12

0.128

-

stomach

0.13

0.15

0.158

-

small intestine

0.159

-

microsomal rhodanese 28 days after common bile duct ligation

0.18

0.183

-

liver

0.19

-

rhodanese activity in muscle of reticulum of rumen of female animals

0.21

-

rhodanese activity in fundus muscle of abomasum of male animals

0.214

-

liver

0.22

-

rhodanese activity in fundus muscle of abomasum of female animals

0.23

-

rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of cysteine

0.24

0.246

-

left colon

0.25

4 entries

0.254

-

rectum

0.26

0.28

0.289

-

microsomal rhodanese 28 days after apparent operation

0.29

-

rhodanese activity in small intestine of female animals

0.292

-

right colon

0.3

-

rhodanese activity in heart ventricle of female animals

0.31

0.314

-

liver

0.32

0.34

-

rhodanese activity in heart ventricle of male animals

0.35

0.36

0.362

-

rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-2,4-dicarboxylic acid

0.37

0.374

-

rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-4-carboxylic acid

0.376

-

rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of methionine

0.38

-

rhodanese activity in heart atrium of male animals

0.39

-

rhodanese activity in heart atrium of female animals

0.4

-

rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiocystine

0.426

-

kidney

0.47

0.476

-

rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiazolidine-4-carboxylic acid

0.48

-

enzyme from brain, pH 9.2, 37°C

0.49

-

rhodanese activity in brain of female animals

0.51

-

rhodanese activity in fundus epithelium of abomasum of male animals

0.52

-

rhodanese activity in fundus epithelium of abomasum of female animals

0.56

0.57

-

rhodanese activity in pylore epithelium of abomasum of female animals

0.59

-

muscle

0.6

-

rhodanese activity in large intestine of male animals

0.619

-

kidney

0.62

-

rhodanese activity in large intestine of male animals

0.63

Manihot esculenta

-

preparative PAGE

645512

0.67

-

spleen

0.82

-

enzyme from kidney cortex, pH 9.2, 37°C

0.88

-

kidney

0.903

-

liver

0.94

0.965

-

enzyme from kidney, pH 9.2, 37°C

0.97

-

rhodanese activity in kidney cortex of female animals

1.03

-

cytosolic rhodanese 42 days after common bile duct ligation

1.06

-

cytosolic rhodanese 28 days after common bile duct ligation

1.08

-

mitochondrial rhodanese 42 days after common bile duct ligation

1.11

-

cytosolic rhodanese 14 days after common bile duct ligation

1.14

-

mitochondrial rhodanese 28 days after common bile duct ligation

1.2

-

1.25

-

liver

1.35

-

cytosolic rhodanese 28 days after common bile duct ligation

1.4

Equus caballus

-

enzyme from kidney, pH 9.2, 37°C

1.68

-

mitochondrial rhodanese 28 days after common bile duct ligation

1.7

1.83

-

cytosolic rhodanese 7 days after common bile duct ligation

10.3

-

enzyme from epithelial layer of rumen, pH 9.2, 37°C

1071

-

after Sephacryl S-200-HR gel filtration

15.9

-

Sephadex G-100

16.3

-

enzyme from epithelial layer of rumen, pH 9.2, 37°C

2.18

-

mitochondrial rhodanese 14 days after common bile duct ligation

2.27

-

cytosolic rhodanese 3 days after common bile duct ligation

2.44

-

mitochondrial rhodanese 7 days after common bile duct ligation

2.5

-

cytosolic rhodanese 2 days after common bile duct ligation

2.6

pH 7.4, 37°C

2.61

-

cytosolic rhodanese 1 day after common bile duct ligation

2.85

-

cytosolic rhodanese 12 h after common bile duct ligation

2.93

2.99

-

rhodanese activity in omasum of male animals

21

-

645532

225

-

recombinant wild-type enzyme

Rhodopseudomonas palustris

242

Chlorocebus aethiops

-

645499

297.9

-

645497

3

3.06

-

cytosolic rhodanese 12 h after apparent operation

3.07

-

cytosolic rhodanese 14 and 42 days after apparent operation

3.08

-

cytosolic rhodanese 3 days after apparent operation

3.09

-

cytosolic rhodanese 7 and 28 days after apparent operation

3.1

-

cytosolic rhodanese 1 and 2 days after apparent operation

3.14

-

rhodanese activity in reticulum of rumen of female animals

3.25

-

mitochondrial rhodanese 3 days after common bile duct ligation

3.31

3.63

-

cytosolic rhodanese 28 days after apparent operation

3.76

3.82

-

rhodanese activity in epithelium of omasum of female animals

332

-

wild-type

353

-

Ser-1

389

-

Ser-2

391

-

one additional Arg residue at the 3'-end followed by a TAA stop codon

4.02

-

mitochondrial rhodanese 1 day after common bile duct ligation

4.16

-

rhodanese activity in rumen of male animals

4.18

-

mitochondrial rhodanese 12 h after common bile duct ligation

4.23

-

rhodanese activity in rumen of female animals

4.25

-

mitochondrial rhodanese 7 and 42 days after apparent operation

4.26

-

mitochondrial rhodanese 14 and 28 days after apparent operation

4.3

-

mitochondrial rhodanese 2 and 3 days after apparent operation

4.31

-

mitochondrial rhodanese 1 day after apparent operation

4.35

-

mitochondrial rhodanese 12 h after apparent operation

4.64

-

mitochondrial rhodanese 28 days after apparent operation

4.95

-

enzyme from liver, pH 9.2, 37°C

440

-

T232A

491

Oncorhynchus mykiss

-

C-terminally extended mutant enzyme

5

-

rhodanese activity in epithelium of reticulum of rumen of female animals

5.08

-

rhodanese activity in epithelium of reticulum of rumen of male animals

5.21

-

enzyme from liver, pH 9.2, 37°C

550

-

T232K

575.5

-

R186L

6

-

600

-

main fraction of Sephadex G-200 gel chromatography

645511

672.8

-

wild-type

645527

70

-

QAE-Sephadex column II

700

-

preparative polyacrylamide gel electrophoresis

720

-

730

-

purificated liver rhodanese

645508

8.92

-

rhodanese activity in epithelium of rumen of female animals

8.99

-

rhodanese activity in epithelium of rumen of male animals

816

818

Oncorhynchus mykiss

-

recombinant wild-type

85.3

-

substrate thiosulfate, pH 9.2, 22°C

673274

850

-

pH 9.0, 80°C

additional information

10.5

-

strain O82

11

-

11.5

-

strain O80

6.5

-

mitochondria

7 - 8.5

-

7.5

7.5 - 8.5

-

8 - 8.5

-

8.5 - 10.5

-

strain O90 and strain O77

8.5 - 11.5

-

strain O10

9

9.4

-

additional information

-

cytoplasmic enzyme exhibits a more acidic pH-optimum than the mitochondrial enzyme

645538

5.5 - 10.5

-

pH 5.5: about 45% of maximal activity, pH 10.5: about 95% of maximal activity, pH 11.0: about 15% of maximal activity

6 - 11

-

pH 6.0: about 75% of activity maximum, pH 11.0: about 70% of activity maximum

7

-

no residual activity below

20

20 - 32

25

-

30

35

35 - 55

-

strain O90

45

-

strain O10 and strain O82

50

-

60

-

73

-

mitochondrial and cytosolic enzyme of untreated mice

80

-

0 - 50

-

25

-

8% of maximum activity

4.7 - 4.8

-

645496

5

-

isoelectrophoresis in polyacrylamide gels, cytosol

5.1

-

5.3

-

isoelectrophoresis in polyacrylamide gels, mitochondria

645498

6.6

-

isoelectric focusing in Phast Gel isoelectric focusing gel with pH range: 3 - 9

Acidithiobacillus ferrooxidans

-

-

-

-

Brassica rapa subsp. rapa

-

-

-

-

cabbage

-

-

-

Canis lupus familiaris

-

-

vervet monkey

-

Columbia domesticus

-

Desulfotomaculum nigrificans

-

-

-

-

-

comparison of enzyme activity with several tissues of sheep, cattle, goat, camel, dog, chicken and human

-

-

645502, 645518, 645532, 645533

-

-

-

-

-

-

-

-

-

-

-

Mycobacterium tuberculosis H37Rv

Oncorhynchus mykiss

chinese hamster

Rhodopseudomonas palustris

-

Oryctolagus cuniculus

-

-

parsley

-

Pseudomonas aeruginosa

-

-

-

-

serovar typhimurium

-

spinach

-

Staphylococcus aureus

-

737706

-

Starkeya novella

-

645502, 645516

-

Thiobacillus denitrificans

-

-

-

-

strains: O90, O77, O10, O82, O80

Ehrlich ascites carcinoma cell

-

Xylella fastidiosa

-

760422

-

Xylella fastidiosa 9a5c

-

-

-

-

-

-

-

-

atrium and ventricle

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

additional information

endoplasmic reticulum

-

muscle and epithelium

-

-

malfunction

metabolism

a mitochondrial sulfur catabolic pathway catalyzes the complete oxidation of L-cysteine to pyruvate and thiosulfate. After transamination to 3-mercaptopyruvate, the sulfhydryl group from L-cysteine is transferred to glutathione by sulfurtransferase Str1 and oxidized to sulfite by the sulfur dioxygenase Ethe1. Sulfite is then converted to thiosulfate by addition of a second persulfide group by sulfurtransferase 1. This pathway is most relevant during early embryo development and for vegetative growth under light-limiting conditions

762111

physiological function

7 entries

Escherichia coli BL21(DE3)

Escherichia coli K-12

4 entries

Mycolicibacterium thermoresistibile

3p3a, download, 3D-view

SCOPe (3p3a)

CATH (3p3a)

E2QRA0

Paraburkholderia phytofirmans PsJN

1yt8, download, 3D-view

SCOPe (1yt8)

CATH (1yt8)

Q9I0N4

Pseudomonas aeruginosa

3d1p, download, 3D-view

SCOPe (3d1p)

CATH (3d1p)

Q12305

Saccharomyces cerevisiae

Saccharomyces cerevisiae S288C

1uar, download, 3D-view

11000

-

x * 11000, SDS-PAGE

645533

12100

-

alpha2, 2 * 12100, calculated from nucleotide sequence and SDS-PAGE

12800

12804

14000

-

gel filtration, autooxidation to a polymeric form which is probably an inert dimer

645518

15000

Rhodopseudomonas palustris

-

4 * 15000, calculated from amino acid sequence

15000 - 50000

-

16000

-

alphabeta, 1 * 16000 + 1 * 17000, SDS-PAGE

645512

16500

-

645497

17000

18000

-

4 * 18000, SDS-PAGE

724480

18500

-

alpha2, 2 * 18500, crystallographic data

645504

19000

-

alpha2, 2 * 19000, SDS-PAGE

20300

-

gel filtration, cytosol

645498

21600

Staphylococcus aureus

-

737706

22500

-

gel filtration

645532

29000

-

calculated from the amino acid composition

32000

33000

33000 - 34000

-

hydrophobic column chromatography

334000

-

x * 334000, MALDI-TOF mass spectrometry

725406

34000

-

1 * 34000, SDS-PAGE

34800

-

gel filtration

35000

-

gel filtration

36000

-

gel filtration

37000

37500

-

sedimentation velocity-diffusion method

38000

Starkeya novella

-

alpha2, 2 * 38000, SDS-PAGE

645516

51700

-

gel filtration

65000

-

SDS-PAGE

724480

74000

P9WHF9

gel filtratioin

762459

78000

Starkeya novella

-

gel filtration

645516

9000

-

gel filtration, mitochondria

?

dimer

homotetramer

monomer

tetramer

-

4 * 12804, calculated, 4 * 12800, mass spectrometry, enzyme is in equilibrium between monomer, dimer and tetramer with shift to the tetrameric state in presence of substrate

additional information

homology modeling of structure. The potential active site is located between a central beta strand and an alpha helix. Residues R30, E34 are involved in substrate binding

-

solution structure of enzyme detected by NMR spectroscopy. Enzyme contains an additional beta-hairpin not found in other rhodaneses. the enzyme atically active domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases and stress proteins

Arabidopsis thaliana

Q39129

677018

composed of two identically folded domains with 13 and 21% identical residues

-

645543

in the sulfur-free state the catalytic Cys residue adopts two alternate conformations, catalytic mechanism relies primarily on the main-chain conformation of the 230 to 235 active-site loop and on a surrounding strong positive electrostatic field

-

-

at 2 mM (NH4)2SO4 soluble enzyme has low activity and crystals are stable when substrates are added, at 1.4 mM (NH4)2SO4 crystals rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O32-

-

645510

composed of two identically folded domains with 13 and 21% identical residues

-

645543

crystallization in a solution with (NH4)2SO4 at pH 7.3, space group C2 with a: 156.0 A, b: 49.0 A, c: 42.2 A and beta: 98.3°

-

645504

crystallization in a solution with (NH4)2SO4 at pH 7.9

-

645501

the model contains 2327 protein atoms and 407 solvent molecules, replacement of the precipitant (NH4)2SO4 with cryoprotectants in the crystal-suspending medium led to the removal of the sulfate ion from the enzyme active site

-

645545

wild-type and DELTA1-7 in polyethyleneglycol 6000, the two-domain structure is not significantly altered by drastically different crystallization conditions or crystal packing, sitting-drop vapour-diffusion method, orthorhombic crystal

-

645526

1.04 A resolution crystal structure displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase

Q8NFU3

761486

sitting-drop vapour-diffusion method

-

690262

structure of CysA2 at 2.29 A shows two alpha/beta domains. The N domain is inactive, whereas the C domain is responsible for the catalytic activity. The conserved catalytic cysteine of the active site is Cys233

P9WHF9

762459

C332S

Arabidopsis thaliana

-

mutation leads to higher rigidity of the molecule

672482

C339V

Arabidopsis thaliana

-

no conformational changes

672482

T232A

-

increase in thiosulfate-cyanide sulfurtransferase activity and no activity with 3-mercaptopyruvate as sulfur donor

T232K

-

increase in thiosulfate-cyanide sulfurtransferase activity and no activity with 3-mercaptopyruvate as sulfur donor

Arg

-

one additional Arg residue at the 3'-end followed by a TAA stop codon, no significant changes to the wild-type enzyme

C247S

-

no activity to thiosulfate

C254S

-

more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur

C254S/C263S

-

less stable in urea than wild type, more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur

C263S

-

less stable in urea than wild type

C3S

-

mutant enzyme is fully active but less stable than wild-type enzyme, mutant enzyme has more easily exposed apparent hydrophobic surfaces than wild-type enzyme

663321

C63S

-

less stable in urea than wild type

C63S/C254S/C263S

-

less stable in urea than wild type, more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur

DELTA1-3

-

no significant change in stability versus wild-type

DELTA1-7

K249A

R186L

-

increased KM for thiosulfate

645527

Ser-1

-

one additional Ser residue at the 3'-end followed by a TAA stop codon, loss of enzymatic activity above 30°C

Ser-2

-

one additional Ser residue at the 3'-end followed by a TAG stop codon, loss of enzymatic activity above 30°C

E102D

-

natural polymorphism, slight decrease both in Vmax and Km value

677214

P285A

-

natural polymorphism, ratio of Vmax to Km value is decreased by 50%

677214

C266S

Xylella fastidiosa

-

activity is completely abolished, similar to wild-type, mutant is able to form high molecular weight oligomers (> 600 kDa)

760422

C33S

Xylella fastidiosa

-

about 3fold increase in sulfurtransferase activity, mutation destabilizes the quaternary structure

760422

C266S

Xylella fastidiosa 9a5c

-

activity is completely abolished, similar to wild-type, mutant is able to form high molecular weight oligomers (> 600 kDa)

-

C33S

Xylella fastidiosa 9a5c

-

about 3fold increase in sulfurtransferase activity, mutation destabilizes the quaternary structure

-

additional information

7 entries

4 - 8

-

30°C, 44 h, stable

645513

9 - 13

-

stable

645517

30

-

60 min, stable

40

-

60 min, about 40% loss of activity

50

58.3

melting temperature

60

70

-

10 min, pH 5.0, stable up to

at 1.4 M ammonium sulfate, crystals rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O32-

-

645510

at 2 M ammonium sulfate, crystals of the enzyme are stable when substrates are added

-

645510

dithithreitol prevents enzyme inhibition by NO-donors and fully restores catalytic activity

-

645521

mutant enzyme C3S is inactivated by bis(1,8-anilinonaphthalenesulfonate) in the light, bis(1,8-anilinonaphthalenesulfonate) is photo-incorporated into the C-terminal domain of C3S and makes the mutant enzyme less stable, binding to wild-type enzyme is very slow

-

663321

-20°C, several months

-

-70°C, 3 weeks, enzyme splits in two identical subunits with a molecular weight of 17000 Da

-

-

15 entries

bovine liver and recombinant Escherichia coli BL21(DE3) enzyme

-

GlpE

-

HisTrap column

-

690262

lwoffi

-

partial

PspE

-

recombinant N-terminal domain

-

661748

-

Pseudomonas aeruginosa

-

660889

cloning and overexpression of the N-terminal domain of the protein

-

661748

expression in a cell free Escherichia coli system by coupled transcription/translation

-

645529, 645543

expression in Escherichia coli

expression in Escherichia coli BL21(DE3)

-

645508

expression of His6-Rv3117 in Escherichia coli BL21-DE3

-

690262

expression of PspE in Escherichia coli

-

645533

overexpression in Escherichia coli BL-21

-

645523

overexpression in Escherichia coli M15

-

transient expression in cos-7 and 293 cells and expression in Escherichia coli XL1 B

P00586

645509

hemodialysis patients show significantly lower rhodanese mRNA and protein expression

-

724781

the expression of the aq-1599 gene is induced in the presence of elemental sulfur

-

724480

the hepatic and renal enzyme activity increases by 0.5 LD50 potassium cyanide

-

-

-

refolds from 8 M urea to enzymatically active species

-

645508, 645527

translation elongation factor EF-Tu enhances renaturation of rhodanese after treatment with 8 mM urea

-

645543

analysis

-

detection method for cyanide based on in-capillary enzymic reaction. Method shows a linear detection range from 0.015 to 0.5 mM with a detection limit of 0.003 mM and a limit of quantitation of 0.09 mM. The method is rapid, simple and can easily be automated

675044

medicine

7 entries

pharmacology