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Literature summary extracted from
- Crystal structure of S-adenosyl-L-homocysteine hydrolase from Cytophaga hutchinsonii, a case of combination of crystallographic and non-crystallographic symmetry (2018), Croat. Chem. Acta, 91, 153-162 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.13.2.1 | expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells | Cytophaga hutchinsonii |
| 3.13.2.1 | expression in Escherichia coli BL21 | Cytophaga hutchinsonii |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.13.2.1 | enzyme in ternary complex with the oxidized form of the NAD+ cofactor and adenosine, hanging drop vapor diffusion method, using 15 % (w/v) PEG 8000 and 0.5 M Li2SO4 | Cytophaga hutchinsonii |
| 3.13.2.1 | hanging-drop vapor-diffusion method, crystals are orthorhombic, space group P2(1)2(1)2 with unit cell parameters a = 96.28, b = 102.44, and c = 188.92 A | Cytophaga hutchinsonii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.13.2.1 | 0.0152 | - |
S-adenosyl-L-homocysteine | pH 7.5, 22°C | Cytophaga hutchinsonii |  |
| 3.13.2.1 | 0.0152 | - |
S-adenosyl-L-homocysteine | at pH 7.5 and 22°C | Cytophaga hutchinsonii | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.13.2.1 | Na+ | contains a sodium cation in close proximity of the active site | Cytophaga hutchinsonii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.13.2.1 | 200000 | - |
gel filtration | Cytophaga hutchinsonii |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.13.2.1 | L-homocysteine + adenosine | Cytophaga hutchinsonii | - |
S-adenosyl-L-homocysteine + H2O | - |
r | |
| 3.13.2.1 | L-homocysteine + adenosine | Cytophaga hutchinsonii ATCC 33406 | - |
S-adenosyl-L-homocysteine + H2O | - |
r | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | Cytophaga hutchinsonii | - |
L-homocysteine + adenosine | - |
? | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | Cytophaga hutchinsonii | - |
L-homocysteine + adenosine | - |
r | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | Cytophaga hutchinsonii ATCC 33406 | - |
L-homocysteine + adenosine | - |
? | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | Cytophaga hutchinsonii ATCC 33406 | - |
L-homocysteine + adenosine | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.13.2.1 | Cytophaga hutchinsonii | A0A6N4SNR7 | - |
- |
| 3.13.2.1 | Cytophaga hutchinsonii ATCC 33406 | A0A6N4SNR7 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.13.2.1 | HisTrap column chromatography and Superdex S200 gel filtration | Cytophaga hutchinsonii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.13.2.1 | L-homocysteine + adenosine | - |
Cytophaga hutchinsonii | S-adenosyl-L-homocysteine + H2O | - |
r | |
| 3.13.2.1 | L-homocysteine + adenosine | - |
Cytophaga hutchinsonii ATCC 33406 | S-adenosyl-L-homocysteine + H2O | - |
r | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | - |
Cytophaga hutchinsonii | L-homocysteine + adenosine | - |
? | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | - |
Cytophaga hutchinsonii | L-homocysteine + adenosine | - |
r | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | - |
Cytophaga hutchinsonii ATCC 33406 | L-homocysteine + adenosine | - |
? | |
| 3.13.2.1 | S-adenosyl-L-homocysteine + H2O | - |
Cytophaga hutchinsonii ATCC 33406 | L-homocysteine + adenosine | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.13.2.1 | tetramer | 4 * 48000, SDS-PAGE | Cytophaga hutchinsonii |
| 3.13.2.1 | tetramer | the asymmetric unit of the enzyme (ChSAHase) crystal contains four subunits of the enzyme. They do not form one functional tetrameric unit. They are assembled into two dimers, located at two different crystallographic twofold axes, whose operation recreates two tetramers that are related by non-crystallographic translation | Cytophaga hutchinsonii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.13.2.1 | S-adenosyl-L-homocysteine hydrolase | - |
Cytophaga hutchinsonii |
| 3.13.2.1 | SAHase | - |
Cytophaga hutchinsonii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.13.2.1 | 0.042 | - |
S-adenosyl-L-homocysteine | pH 7.5, 22°C | Cytophaga hutchinsonii | |
| 3.13.2.1 | 0.042 | - |
S-adenosyl-L-homocysteine | at pH 7.5 and 22°C | Cytophaga hutchinsonii | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.13.2.1 | NAD+ | - |
Cytophaga hutchinsonii | |
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