Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21(DE3) cells | Xylella fastidiosa |
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Xylella fastidiosa |
Crystallization (Comment) | Organism |
---|---|
enzyme bound to N-acetyl-L-glutamate, sitting drop vapor diffusion method, using 0.2 M Li2SO4, 0.1 M Tris pH 6.5, 25% (w/v) PEG 3350 | Xylella fastidiosa |
purified recombinant N-acetyltransferase domain of N-acetyl-L-glutamate synthase/kinase, with and without a His-tag, complexed with N-acetyl-L-glutamate, sitting-drop vapor-diffusion method, 0.002 ml of protein in 50 mM Tris-HCl, pH 7.4, 50 mM NaCl, 10% glycerol, 5 mM 2-mercaptoethanol, 1 mM EDTA, 10 mM CoA, and 10 mM N-acetyl-L-glutamate, is mixed with 0.2 M Li2SO4, 0.1 M Tris, pH 6.5, 25% PEG 3350 for the His-tagged enzyme, and with 0.2 M Li2SO4, 0.1 M Tris, pH 8.5, 25% PEG 3350 for the detagged enzyme, X-ray diffraction structure determination and analysis at 1.7 A and 1.4 A resolution, respectively | Xylella fastidiosa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37400 | - |
catalytic N-acetyltransferase domain, gel filtration | Xylella fastidiosa |
37400 | - |
recombinant dimeric N-acetyltransferase domain, gel filtration | Xylella fastidiosa |
38800 | - |
catalytic N-acetyltransferase domain, calculated from amino acid sequence | Xylella fastidiosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-glutamate | Xylella fastidiosa | - |
CoA + N-acetyl-L-glutamate | - |
? | |
acetyl-CoA + L-glutamate | Xylella fastidiosa ATCC 35881D | - |
CoA + N-acetyl-L-glutamate | - |
? | |
additional information | Xylella fastidiosa | the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview | ? | - |
? | |
additional information | Xylella fastidiosa ATCC 35881D | the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xylella fastidiosa | - |
- |
- |
Xylella fastidiosa | Q87EL2 | - |
- |
Xylella fastidiosa ATCC 35881D | - |
- |
- |
Purification (Comment) | Organism |
---|---|
HiTrap column chromatography | Xylella fastidiosa |
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and cation exchange chromatography, the His-tag is cleaved by thrombin | Xylella fastidiosa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-glutamate | - |
Xylella fastidiosa | CoA + N-acetyl-L-glutamate | - |
? | |
acetyl-CoA + L-glutamate | - |
Xylella fastidiosa ATCC 35881D | CoA + N-acetyl-L-glutamate | - |
? | |
additional information | the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview | Xylella fastidiosa | ? | - |
? | |
additional information | the bifunctional N-acetyl-L-glutamate synthase/kinase contains an N-terminal catalytic N-acetyltransferase (NAT) domain, substrate N-acetyl-l-glutamate binding structure analysis, overview | Xylella fastidiosa ATCC 35881D | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | isolated N-acetyltransferase domain of N-acetyl-L-glutamate synthase/kinase | Xylella fastidiosa |
homodimer | x-ray crystallography | Xylella fastidiosa |
More | eight subunits of N-acetyltransferase domain form four molecular dimers in the crystal structure, overview | Xylella fastidiosa |
Synonyms | Comment | Organism |
---|---|---|
N-acetyl-L-glutamate synthase/kinase | - |
Xylella fastidiosa |
N-acetyl-L-glutamate synthase/kinase | bifunctional enzyme | Xylella fastidiosa |
NAGS | - |
Xylella fastidiosa |
NAGS/K | - |
Xylella fastidiosa |
NAT | catalytic N-acetyltransferase domain | Xylella fastidiosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Xylella fastidiosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Xylella fastidiosa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Xylella fastidiosa |