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Literature summary for 3.2.2.16 extracted from
- Mechanism of substrate specificity in 5-methylthioadenosine/S-adenosylhomocysteine nucleosidases (2011), J. Struct. Biol., 173, 86-98.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| isozyme AtMTAN1, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) | Arabidopsis thaliana |
| overexpression of wild-type and mutant His-tagged enzyme in strain BL21(DE3) | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure comparison of MTAN from Escherichia coli with the isozyme AtMTAN1 from Arabidopsis thaliana, overview | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E174Q | site-directed mutagenesis, structure comparison with the wild-type enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics and thermodynamics, overview | Escherichia coli | |
| additional information | - |
additional information | kinetics and thermodynamics, overview | Arabidopsis thaliana |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Arabidopsis thaliana | AtMTAN2 is dual-substrate specific and is responsible for the hydrolysis of 5'-methylthioadenosine and S-adenosylhomocysteine to adenine and their corresponding thioriboses, overview | ? | - |
? |  |
| additional information | Escherichia coli | MTAN is dual-substrate specific and is responsible for the hydrolysis of 5'-methylthioadenosine and S-adenosylhomocysteine to adenine and their corresponding thioriboses, overview | ? | - |
? | |
| S-methyl-5'-thioadenosine + H2O | Escherichia coli | - |
S-methyl-5-thio-D-ribose + adenine | - |
? | |
| S-methyl-5'-thioadenosine + H2O | Arabidopsis thaliana | - |
S-methyl-5-thio-D-ribose + adenine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
isozyme AtMTAN1 | - |
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged isozyme AtMTAN1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Arabidopsis thaliana |
| recombinant wild-type and mutant His-tagged MTAN from strain BL21(DE3) by nickel affinity chromatography | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
amide proton exchange rates of isozyme AtMTAN1 | Arabidopsis thaliana |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | AtMTAN2 is dual-substrate specific and is responsible for the hydrolysis of 5'-methylthioadenosine and S-adenosylhomocysteine to adenine and their corresponding thioriboses, overview | Arabidopsis thaliana | ? | - |
? | |
| additional information | MTAN is dual-substrate specific and is responsible for the hydrolysis of 5'-methylthioadenosine and S-adenosylhomocysteine to adenine and their corresponding thioriboses, overview | Escherichia coli | ? | - |
? | |
| additional information | dynamics are an important factor in substrate selection in MTAN, overview. Substrate binding induces a favourable entropic change in AtMTAN1 | Arabidopsis thaliana | ? | - |
? | |
| additional information | substrate binding, specificity and dynamics, overview. Substrate binding induces a unfavourable entropic change | Escherichia coli | ? | - |
? | |
| S-methyl-5'-thioadenosine + H2O | - |
Escherichia coli | S-methyl-5-thio-D-ribose + adenine | - |
? | |
| S-methyl-5'-thioadenosine + H2O | - |
Arabidopsis thaliana | S-methyl-5-thio-D-ribose + adenine | - |
? | |
| S-methyl-5'-thioadenosine + H2O | preferred substrate | Arabidopsis thaliana | S-methyl-5-thio-D-ribose + adenine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | structure comparison of isozyme AtMTAN1 with the MTAN from Escherichia coli, overview | Arabidopsis thaliana |
| More | structure comparison of MTAN from Escherichia coli with isozyme AtMTAN from Arabidopsis thaliana, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase | - |
Escherichia coli |
| 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase | - |
Arabidopsis thaliana |
| MTA/SAH nucleosidase | - |
Escherichia coli |
| MTA/SAH nucleosidase | - |
Arabidopsis thaliana |
| MTAN | - |
Escherichia coli |
| MTAN | - |
Arabidopsis thaliana |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
| 7.5 | - |
assay at | Arabidopsis thaliana |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase plays a key role in the methionine-recycling pathway of bacteria and plants | Escherichia coli |
| metabolism | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase plays a key role in the methionine-recycling pathway of bacteria and plants | Arabidopsis thaliana |
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Release 2023.1 (January 2023)
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