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Literature summary extracted from

  • Mishra, V.; Ronning, D.R.
    Crystal structures of the Helicobacter pylori MTAN enzyme reveal specific interactions between S-adenosylhomocysteine and the 5-alkylthio binding subsite (2012), Biochemistry, 51, 9763-9772.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.9 expressed in Escherichia coli BL21(DE3) Rosetta cells Helicobacter pylori
3.2.2.16 expressed in Escherichia coli BL21 (DE3) Rosetta cells Helicobacter pylori
3.2.2.30 expressed in Escherichia coli BL21(DE3) Rosetta cells Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.9 hanging drop vapor diffusion method. Inactive D198N mutant bound to S-adenosyl-L-homocysteine and active enzyme bound to S-(5-deoxy-D-ribos-5-yl)-L-homocysteine and adenine using 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES (pH 7.5), and 30% (v/v) PEG-MME 550 Helicobacter pylori
3.2.2.16 hanging drop vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M HEPES pH 7.5 and 25% (w/v) PEG 3350 or 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5 and 30% (v/v) PEG-MME 550 Helicobacter pylori
3.2.2.30 hanging drop vapor diffusion method. Inactive D198N mutant bound to 5'-methylthioadenosine using 0.2 M magnesium chloride, 0.1 M HEPES (pH 7.5), and 25% (w/v) PEG 3350 Helicobacter pylori

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.16 D198N inactive Helicobacter pylori
3.2.2.16 F107A the mutant shows reduced activity compared to the wild type enzyme Helicobacter pylori
3.2.2.16 H109A the mutant shows reduced activity compared to the wild type enzyme Helicobacter pylori
3.2.2.30 D198N inactive Helicobacter pylori

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.9 0.01
-
S-adenosyl-L-homocysteine wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.9 0.014
-
S-adenosyl-L-homocysteine mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.9 0.019
-
S-adenosyl-L-homocysteine mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.16 0.01
-
S-adenosyl-L-homocysteine wild type enzyme, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 0.014
-
S-adenosyl-L-homocysteine mutant enzyme H109A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 0.019
-
S-adenosyl-L-homocysteine mutant enzyme F107A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 0.033
-
S-methyl-5'-thioadenosine mutant enzyme H109A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 0.037
-
S-methyl-5'-thioadenosine mutant enzyme F107A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 0.039
-
S-methyl-5'-thioadenosine wild type enzyme, at pH 7.2 and 25°C Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.9 S-adenosyl-L-homocysteine + H2O Helicobacter pylori
-
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
-
?
3.2.2.16 5'-deoxyadenosine + H2O Helicobacter pylori
-
5-deoxy-D-ribose + adenine
-
?
3.2.2.16 6-amino-6-deoxyfutalosine + H2O Helicobacter pylori
-
3-{3-[(2R,3S,4R,5R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoic acid + 9H-purine-6-amine
-
?
3.2.2.16 S-adenosyl-L-homocysteine + H2O Helicobacter pylori
-
S-ribosyl-L-homocysteine + adenine
-
?
3.2.2.16 S-methyl-5'-thioadenosine + H2O Helicobacter pylori
-
S-methyl-5-thio-D-ribose + adenine
-
?
3.2.2.30 6-amino-6-deoxyfutalosine + H2O Helicobacter pylori
-
dehypoxanthine futalosine + adenine
-
?
3.2.2.30 additional information Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is a multifunctional enzyme that catalyzes the hydrolysis of the N-ribosidic bond of at least four different adenosine-based metabolites: S-adenosyl-L-homocysteine, 5'-methylthioadenosine, 5'-deoxyadenosine, and 6-amino-6-deoxyfutalosine ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.9 Helicobacter pylori
-
-
-
3.2.2.16 Helicobacter pylori Q9ZMY2
-
-
3.2.2.30 Helicobacter pylori
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.9 HisTrap column chromatography and Superdex 200 gel filtration Helicobacter pylori
3.2.2.16 HisTrap column chromatography and Superdex 200 gel filtration Helicobacter pylori
3.2.2.30 HisTrap column chromatography and Superdex 200 gel filtration Helicobacter pylori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.9 S-adenosyl-L-homocysteine + H2O
-
Helicobacter pylori S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
-
?
3.2.2.16 5'-deoxyadenosine + H2O
-
Helicobacter pylori 5-deoxy-D-ribose + adenine
-
?
3.2.2.16 6-amino-6-deoxyfutalosine + H2O
-
Helicobacter pylori 3-{3-[(2R,3S,4R,5R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoic acid + 9H-purine-6-amine
-
?
3.2.2.16 S-adenosyl-L-homocysteine + H2O
-
Helicobacter pylori S-ribosyl-L-homocysteine + adenine
-
?
3.2.2.16 S-methyl-5'-thioadenosine + H2O
-
Helicobacter pylori S-methyl-5-thio-D-ribose + adenine
-
?
3.2.2.30 6-amino-6-deoxyfutalosine + H2O
-
Helicobacter pylori dehypoxanthine futalosine + adenine
-
?
3.2.2.30 additional information 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is a multifunctional enzyme that catalyzes the hydrolysis of the N-ribosidic bond of at least four different adenosine-based metabolites: S-adenosyl-L-homocysteine, 5'-methylthioadenosine, 5'-deoxyadenosine, and 6-amino-6-deoxyfutalosine Helicobacter pylori ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.2.9 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
Helicobacter pylori
3.2.2.9 MTAN
-
Helicobacter pylori
3.2.2.16 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
Helicobacter pylori
3.2.2.16 MTAN
-
Helicobacter pylori
3.2.2.30 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
Helicobacter pylori
3.2.2.30 MTAN
-
Helicobacter pylori

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.2.9 0.44
-
S-adenosyl-L-homocysteine mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.9 0.74
-
S-adenosyl-L-homocysteine mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.9 1.8
-
S-adenosyl-L-homocysteine wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.16 0.44
-
S-adenosyl-L-homocysteine mutant enzyme F107A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 0.74
-
S-adenosyl-L-homocysteine mutant enzyme H109A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 1
-
S-methyl-5'-thioadenosine mutant enzyme F107A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 1.2
-
S-methyl-5'-thioadenosine mutant enzyme H109A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 1.8
-
S-adenosyl-L-homocysteine wild type enzyme, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 3.8
-
S-methyl-5'-thioadenosine wild type enzyme, at pH 7.2 and 25°C Helicobacter pylori

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.2.9 23
-
S-adenosyl-L-homocysteine mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.9 51
-
S-adenosyl-L-homocysteine mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.9 170
-
S-adenosyl-L-homocysteine wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C Helicobacter pylori
3.2.2.16 23
-
S-adenosyl-L-homocysteine mutant enzyme F107A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 27
-
S-methyl-5'-thioadenosine mutant enzyme F107A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 37
-
S-methyl-5'-thioadenosine mutant enzyme H109A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 51
-
S-adenosyl-L-homocysteine mutant enzyme H109A, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 97
-
S-methyl-5'-thioadenosine wild type enzyme, at pH 7.2 and 25°C Helicobacter pylori
3.2.2.16 170
-
S-adenosyl-L-homocysteine wild type enzyme, at pH 7.2 and 25°C Helicobacter pylori