Cloned (Comment) | Organism |
---|---|
N-terminal His6-tagged GluTR expressed in Escherichia coli | Acidithiobacillus ferrooxidans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
SDSPAGE of His6-tagged GluTR | Acidithiobacillus ferrooxidans |
50490 | - |
MALDI-TOF mass spectrometry of His6-tagged GluTR | Acidithiobacillus ferrooxidans |
104000 | - |
cross-linking of GluTR with glutaraldehyde | Acidithiobacillus ferrooxidans |
148000 | - |
relative molecular mass of native recombinant GluTR after removal of His6-tag, determined by gel permeation chromatography | Acidithiobacillus ferrooxidans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acidithiobacillus ferrooxidans | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by Ni2+-Sepharose affinity chromatography to near homogeneity | Acidithiobacillus ferrooxidans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamyl-tRNAGlu + NADPH + H+ | - |
Acidithiobacillus ferrooxidans | L-glutamate 1-semialdehyde + NADP+ + tRNAGlu | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 50000, probably enzyme has an overall V shape that makes the protein migrate slower in gel permeation chromatography | Acidithiobacillus ferrooxidans |
Synonyms | Comment | Organism |
---|---|---|
GluTR | - |
Acidithiobacillus ferrooxidans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | enzyme shows Soret peak at 420 nm and a broad absorbance around 540 nm, data suggest that heme is bound preferentially to the dimeric form of GluTR | Acidithiobacillus ferrooxidans |
General Information | Comment | Organism |
---|---|---|
metabolism | GluTR is the first enzyme committed to tetrapyrrole biosynthesis by the C5-pathway | Acidithiobacillus ferrooxidans |