BRENDA - Reference to 3.6.1.28; Id = 733393

-

Homo sapiens

-

Mus musculus

complex with tripolyphosphate, to 2.3 A resolution and docking solution of substrate thiamine triphosphate. The thiazole ring of the thiamine forms a stacking interaction with Trp53, and the aminopyrimidine ring lies in a pocket defined by His76, Pro191 and Ile195. The triphosphate moiety occupies a similar position as in the enzyme-tripolyphosphate complex, with interactions involving the side chains of Lys11, Arg55, Arg57, Lys65, Arg125 and Lys193

Homo sapiens

D147A

about 30% of wild-type catalytic efficiency

Mus musculus

D37A

about 0.5% of wild-type catalytic efficiency

Mus musculus

E81A

about 30% of wild-type catalytic efficiency

Mus musculus

K11A

about 15% of wild-type catalytic efficiency

Mus musculus

K193A

about 60% of wild-type catalytic efficiency

Mus musculus

K65A

more than 1000fold decrease in kcat value

Mus musculus

W53A

2.5fold increase in catalytic efficiency

Mus musculus

Y39A

about 30% of wild-type catalytic efficiency

Mus musculus

Y79A

about 5% of wild-type catalytic efficiency

Mus musculus

0.008

-

thiamine triphosphate

wild-type, pH 8.5, 37°C

Mus musculus

0.009

-

thiamine triphosphate

mutant K65A, pH 8.5, 37°C

Mus musculus

0.012

-

thiamine triphosphate

mutant K11A, pH 8.5, 37°C

Mus musculus

0.013

-

thiamine triphosphate

mutant E81A, pH 8.5, 37°C

Mus musculus

0.042

-

thiamine triphosphate

mutant Y79A, pH 8.5, 37°C

Mus musculus

0.2

-

thiamine triphosphate

mutant D37A, pH 8.5, 37°C

Mus musculus

0.55

-

thiamine triphosphate

mutant W53A, pH 8.5, 37°C

Mus musculus

0.62

-

thiamine triphosphate

mutant Y39A, pH 8.5, 37°C

Mus musculus

0.74

-

thiamine triphosphate

mutant K193A, pH 8.5, 37°C

Mus musculus

2.8

-

thiamine triphosphate

mutant D147A, pH 8.5, 37°C

Mus musculus

Mg2+

required for catalytic activity, not required for substrate binding

Mus musculus

Homo sapiens

Q9BU02

-

Mus musculus

Q8JZL3

-

thiamine triphosphate + H2O

-

733393

Mus musculus

thiamine diphosphate + phosphate

-

?

Thtpa

-

Homo sapiens

0.019

-

thiamine triphosphate

mutant K65A, pH 8.5, 37°C

Mus musculus

0.64

-

thiamine triphosphate

mutant Y39A, pH 8.5, 37°C

Mus musculus

1.5

-

thiamine triphosphate

mutant K193A, pH 8.5, 37°C

Mus musculus

2.6

-

thiamine triphosphate

mutant D147A, pH 8.5, 37°C

Mus musculus

2.8

-

thiamine triphosphate

mutant D37A, pH 8.5, 37°C

Mus musculus

4.4

-

thiamine triphosphate

mutant W53A, pH 8.5, 37°C

Mus musculus

6

-

thiamine triphosphate

mutant K11A, pH 8.5, 37°C; mutant Y79A, pH 8.5, 37°C

Mus musculus

14.1

-

thiamine triphosphate

mutant E81A, pH 8.5, 37°C

Mus musculus

23

-

thiamine triphosphate

wild-type, pH 8.5, 37°C

Mus musculus

-

Homo sapiens

-

Mus musculus

complex with tripolyphosphate, to 2.3 A resolution and docking solution of substrate thiamine triphosphate. The thiazole ring of the thiamine forms a stacking interaction with Trp53, and the aminopyrimidine ring lies in a pocket defined by His76, Pro191 and Ile195. The triphosphate moiety occupies a similar position as in the enzyme-tripolyphosphate complex, with interactions involving the side chains of Lys11, Arg55, Arg57, Lys65, Arg125 and Lys193

Homo sapiens

D147A

about 30% of wild-type catalytic efficiency

Mus musculus

D37A

about 0.5% of wild-type catalytic efficiency

Mus musculus

E81A

about 30% of wild-type catalytic efficiency

Mus musculus

K11A

about 15% of wild-type catalytic efficiency

Mus musculus

K193A

about 60% of wild-type catalytic efficiency

Mus musculus

K65A

more than 1000fold decrease in kcat value

Mus musculus

W53A

2.5fold increase in catalytic efficiency

Mus musculus

Y39A

about 30% of wild-type catalytic efficiency

Mus musculus

Y79A

about 5% of wild-type catalytic efficiency

Mus musculus

0.008

-

thiamine triphosphate

wild-type, pH 8.5, 37°C

Mus musculus

0.009

-

thiamine triphosphate

mutant K65A, pH 8.5, 37°C

Mus musculus

0.012

-

thiamine triphosphate

mutant K11A, pH 8.5, 37°C

Mus musculus

0.013

-

thiamine triphosphate

mutant E81A, pH 8.5, 37°C

Mus musculus

0.042

-

thiamine triphosphate

mutant Y79A, pH 8.5, 37°C

Mus musculus

0.2

-

thiamine triphosphate

mutant D37A, pH 8.5, 37°C

Mus musculus

0.55

-

thiamine triphosphate

mutant W53A, pH 8.5, 37°C

Mus musculus

0.62

-

thiamine triphosphate

mutant Y39A, pH 8.5, 37°C

Mus musculus

0.74

-

thiamine triphosphate

mutant K193A, pH 8.5, 37°C

Mus musculus

2.8

-

thiamine triphosphate

mutant D147A, pH 8.5, 37°C

Mus musculus

Mg2+

required for catalytic activity, not required for substrate binding

Mus musculus

thiamine triphosphate + H2O

-

733393

Mus musculus

thiamine diphosphate + phosphate

-

?

0.019

-

thiamine triphosphate

mutant K65A, pH 8.5, 37°C

Mus musculus

0.64

-

thiamine triphosphate

mutant Y39A, pH 8.5, 37°C

Mus musculus

1.5

-

thiamine triphosphate

mutant K193A, pH 8.5, 37°C

Mus musculus

2.6

-

thiamine triphosphate

mutant D147A, pH 8.5, 37°C

Mus musculus

2.8

-

thiamine triphosphate

mutant D37A, pH 8.5, 37°C

Mus musculus

4.4

-

thiamine triphosphate

mutant W53A, pH 8.5, 37°C

Mus musculus

6

-

thiamine triphosphate

mutant K11A, pH 8.5, 37°C; mutant Y79A, pH 8.5, 37°C

Mus musculus

14.1

-

thiamine triphosphate

mutant E81A, pH 8.5, 37°C

Mus musculus

23

-

thiamine triphosphate

wild-type, pH 8.5, 37°C

Mus musculus

14

-

thiamine triphosphate

mutant D37A, pH 8.5, 37°C

Mus musculus

140

-

thiamine triphosphate

mutant Y79A, pH 8.5, 37°C

Mus musculus

500

-

thiamine triphosphate

mutant K11A, pH 8.5, 37°C

Mus musculus

1000

-

thiamine triphosphate

mutant D147A, pH 8.5, 37°C; mutant E81A, pH 8.5, 37°C; mutant Y39A, pH 8.5, 37°C

Mus musculus

2000

-

thiamine triphosphate

mutant K193A, pH 8.5, 37°C; mutant K65A, pH 8.5, 37°C

Mus musculus

3000

-

thiamine triphosphate

wild-type, pH 8.5, 37°C

Mus musculus

8000

-

thiamine triphosphate

mutant W53A, pH 8.5, 37°C

Mus musculus

14

-

thiamine triphosphate

mutant D37A, pH 8.5, 37°C

Mus musculus

140

-

thiamine triphosphate

mutant Y79A, pH 8.5, 37°C

Mus musculus

500

-

thiamine triphosphate

mutant K11A, pH 8.5, 37°C

Mus musculus

1000

-

thiamine triphosphate

mutant D147A, pH 8.5, 37°C; mutant E81A, pH 8.5, 37°C; mutant Y39A, pH 8.5, 37°C

Mus musculus

2000

-

thiamine triphosphate

mutant K193A, pH 8.5, 37°C; mutant K65A, pH 8.5, 37°C

Mus musculus

3000

-

thiamine triphosphate

wild-type, pH 8.5, 37°C

Mus musculus

8000

-

thiamine triphosphate

mutant W53A, pH 8.5, 37°C

Mus musculus

751047

Martinez

Structural determinants for s ...

Mus musculus

J. Biol. Chem.

290

23348-23360

2015

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1

-

1

-

1

-

3

-

1

-

2

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-

1

-

1

-

1

-

733393

Delvaux

Structural determinants of spe ...

Homo sapiens, Mus musculus

Biochim. Biophys. Acta

1830

4513-4523

2013

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2

1

9

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10

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1

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2

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1

-

9

-

2

-

1

9

-

10

-

1

-

1

-

9

-

7

687693

Song

Structural basis for the catal ...

Mus musculus

J. Biol. Chem.

283

10939-10948

2008

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1

-

2

-

1

-

2

1

-

1

-

1

-

1

-

2

1

-

1

-

696404

Kovacevic

The iron-regulated metastasis ...

Homo sapiens, Rattus norvegicus

Biochim. Biophys. Acta

1783

1981-1992

2008

2

-

2

-

2

-

2

-

2

-

3

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4

-

4

-

2

-

2

-

2

-

2

-

3

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4

-

667797

Szyniarowski Piot

Pig tissues express a catalyti ...

Homo sapiens, Sus scrofa

Biochim. Biophys. Acta

1725

93-102

2005

-

2

-

4

-

2

3

-

5

2

-

6

-

2

-

1

16

-

2

-

4

-

1

-

5

-

2

-

1

-

2

-

4

-

1

2

3

-

5

2

-

2

-

1

16

-

2

-

1

-

5

-

655738

Lakaye

Human recombinant thiamine tri ...

Homo sapiens

Int. J. Biochem. Cell Biol.

36

1348-1364

2004

-

1

-

6

2

1

2

-

3

-

1

-

1

-

2

-

2

1

-

2

-

1

-

1

-

1

7

2

1

2

-

1

-

1

-

2

-

2

1

-

656873

Czerniecki

Neuronal localization of the 2 ...

Rattus norvegicus

Neuroscience

125

833-840

2004

-

1

-

1

-

4

-

3

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2

-

1

-

1

-

1

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3

-

2

-

668963

Lakaye

Expression of 25 kDa thiamine ...

Mus musculus, Rattus norvegicus

Int. J. Biochem. Cell Biol.

36

2032-2041

2004

-

1

-

5

-

16

-

2

-

4

-

1

-

16

-

2

-

655198

Makarchikov

Thiamine triphosphate and thia ...

Bos taurus, Gallus gallus, Homo sapiens, quail, Rattus norvegicus, Sus scrofa

Cell. Mol. Life Sci.

60

1477-1488

2003

-

15

-

17

-

12

-

25

22

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6

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15

-

17

-

25

22

-

6

-

656042

Lakaye

Molecular characterization of ...

Bos taurus, Homo sapiens

J. Biol. Chem.

277

13771-13777

2002

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1

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4

2

1

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6

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7

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9

2

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4

2

-

2

-

1

-

4

-

2

1

-

6

-

2

-

9

2

-

4

2

-

2

-

210023

Makarchikov

Thiamine triphosphatase activi ...

Bos taurus

Biochem. Mol. Biol. Int.

46

115-123

1998

-

2

-

1

-

2

-

1

-

2

-

1

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2

-

1

-

1

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2

-

1

-

210021

Bettendorff

Thiamine, thiamine phosphates, ...

Homo sapiens

J. Neurochem.

66

250-258

1996

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

210020

Makarchikov

Purification and characterizat ...

Bos taurus

Biochim. Biophys. Acta

1117

326-332

1992

-

1

-

1

6

2

-

2

-

1

-

2

1

2

7

1

-

1

-

1

-

1

6

2

-

1

-

2

1

2

7

1

-

1

-

210012

Matsuda

Membrane-associated thiamine t ...

Rattus norvegicus

Int. J. Biochem.

23

1111-1114

1991

-

9

-

1

-

2

-

2

-

3

-

2

-

9

-

1

-

2

-

3

-

2

-

210022

Bettendorff

Solubilization and thiamine tr ...

Electrophorus electricus

Biochim. Biophys. Acta

1073

69-76

1991

4

-

3

-

1

-

2

-

2

-

1

-

1

-

4

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3

-

1

-

2

-

1

-

1

-

210024

Bettendorff

Application of high-performanc ...

Electrophorus electricus

J. Chromatogr.

566

397-408

1991

-

1

-

1

-

3

-

1

-

2

-

1

-

1

-

1

-

2

-

210019

Nishimune

Hydrolysis and synthesis of th ...

Aneurinibacillus aneurinilyticus, Escherichia coli, Escherichia coli W 1485

J. Nutr. Sci. Vitaminol.

33

113-127

1987

-

3

2

1

-

3

-

3

-

2

-

2

-

1

-

3

1

2

1

-

3

-

2

-

2

-

210018

Ogawa

Recent findings on ultracytoch ...

Rattus norvegicus

Ann. N. Y. Acad. Sci.

378

188-214

1982

-

4

-

1

-

1

-

3

-

2

-

4

-

1

-

3

-

2

-

210017

Penttinen

The relation of the soluble th ...

Rattus norvegicus

Med. Biol.

59

177-184

1981

-

2

-

2

-

7

-

2

-

7

-

210013

Barchi

Membrane-associated thiamin tr ...

Rattus norvegicus

J. Biol. Chem.

251

193-197

1976

-

1

-

1

3

-

1

-

1

-

1

-

1

-

1

3

-

1

-

1

-

210014

Barchi

Membrane thiamine triphosphata ...

Rattus norvegicus

J. Neurochem.

26

715-720

1976

-

4

-

2

-

2

-

2

-

1

-

4

-

2

-

2

-

1

-

210011

Iwata

Properties of thiamine di- and ...

Rattus norvegicus

J. Neurochem.

24

1209-1213

1975

-

4

-

2

-

1

-

1

-

1

-

4

-

2

-

1

-

1

-

210009

Iwata

Role of thiamine metabolism in ...

Rattus norvegicus

Jpn. J. Pharmacol.

24

825-829

1974

-

2

-

1

-

2

-

3

-

1

-

2

-

1

-

3

-

1

-

210010

Iwata

Role of thiamine metabolism in ...

Rattus norvegicus

Jpn. J. Pharmacol.

24

817-823

1974

-

1

-

3

2

-

2

-

3

-

4

-

3

-

1

-

3

2

-

3

-

4

-

3

-

210015

Iwata

-

Some properties of the enzyme ...

Rattus norvegicus

Thiamine (Proc. Pap. U. S. -Jpn. Semin, 2. Meeting)

2. Meeting

213-221

1974

-

4

-

2

-

1

-

2

-

1

-

4

-

2

-

2

-

1

-

210016

Barchi

-

Thiamine triphosphatases in br ...

Rattus norvegicus

Thiamine (Proc. Pap. U. S. -Jpn. Semin, 2. Meeting)

195-212

1974

-

5

2

-

3

-

1

-

1

-

1

-

1

-

1

-

2

-

5

-

2

-

3

-

1

-

1

-

1

-

1

-

2

-

210006

Barchi

A membrane-associated thiamine ...

Rattus norvegicus

J. Biol. Chem.

247

7668-7673

1972

-

3

1

8

1

-

2

-

1

-

8

-

1

-

1

-

2

-

3

-

3

1

8

1

-

1

-

8

-

1

-

1

-

2

-

210007

Hashitani

The partial purification of th ...

Rattus norvegicus

J. Biol. Chem.

247

2117-2119

1972

-

4

1

-

2

-

6

1

-

4

-

4

-

1

-

6

1

-

4

-

210008

Barchi

Thiamine triphosphatase in the ...

Rattus norvegicus

Biochim. Biophys. Acta

255

402-405

1972

1

-

1

-

2

-

1

-

1

-

4

-

1

-

1

-

2

-

1

-

4

-

Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase

Data extracted from this reference: