Cloned (Comment) | Organism |
---|---|
expressed as a His-tagged fusion protein | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
using the hanging-drop vapour diffusion method. SpeE crystals diffract up to 2.9 A resolution using the Quantum 4-CCD detector. SpeE consists of two domains a small N-terminal beta-strand domain, and a C-terminal catalytic domain that adopts a canonical methyltransferase (MTase) Rossmann fold. Structural comparison of Escherichia coli SpeE to its homologs reveals that it has a large and unique substrate-binding cleft that may account for its lower amine substrate specificity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosylmethioninamine + putrescine | - |
Escherichia coli | 5'-S-methyl-5'-thioadenosine + spermidine | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | protein forms a dimer in crystal and solution | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
SpeE | - |
Escherichia coli |
spermidine synthase | - |
Escherichia coli |