Literature summary extracted from
Ma, X.; Zhu, Y.; Lu, J.; Xie, J.; Li, C.; Shin, W.; Qiang, J.; Liu, J.; Dou, S.; Xiao, Y.; Wang, C.; Jia, C.; Long, H.; Yang, J.; Fang, Y.; Jiang, L.; Zhang, Y.; Zhang, S.; Zhai, R.; Liu, C.; Li, D.
Nicotinamide mononucleotide adenylyl transferase uses its NAD+ substrate-binding site to chaperone phosphorylated TAU (2020), eLife, 9, e51859 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.7.1 |
expression in Escherichia coli |
Mus musculus |
2.7.7.1 |
expression in Escherichia coli |
Drosophila melanogaster |
2.7.7.18 |
expression in Escherichia coli |
Mus musculus |
2.7.7.18 |
expression in Escherichia coli |
Drosophila melanogaster |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.7.1 |
structure of NMNAT3 to 2 A resolution |
Mus musculus |
2.7.7.18 |
structure of isoform NMNAT3 to 2 A resolution |
Mus musculus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.7.1 |
E198P/L217R |
mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution |
Mus musculus |
2.7.7.18 |
E198P/L217R |
mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution |
Mus musculus |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.7.7.1 |
64000 |
- |
gel filtration |
Mus musculus |
2.7.7.18 |
64000 |
- |
gel filtration |
Mus musculus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.7.1 |
Drosophila melanogaster |
Q9VC03 |
cf. EC 2.7.7.18 |
- |
2.7.7.1 |
Mus musculus |
Q99JR6 |
isoform NMNAT3, cf. EC 2.7.7.18 |
- |
2.7.7.18 |
Drosophila melanogaster |
Q9VC03 |
cf. EC 2.7.7.1 |
- |
2.7.7.18 |
Mus musculus |
Q99JR6 |
isoform NMNAT3, cf. EC 2.7.7.1 |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.7.1 |
dimer |
2 *27700, calculated from sequence, and crystallization data |
Mus musculus |
2.7.7.18 |
dimer |
2 * 27700, calculated from sequence, and crystallization data |
Mus musculus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.7.1 |
NMNAT3 |
cf. EC 2.7.7.18 |
Mus musculus |
2.7.7.18 |
NMNAT3 |
cf. EC 2.7.7.1 |
Mus musculus |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.7.1 |
physiological function |
NMNAT serves as a chaperone of phosphorylated Tau to prevent its amyloid aggregation in vitro as well as mitigate its pathology in Drosophila tauopathy models overexpressing human Tau. NMNAT adopts its enzymatic pocket to specifically bind the phosphorylated sites of Tau, which can be competitively disrupted by the enzymatic substrates of NMNAT. NMNAT serves as a cochaperone of Hsp90 for the specific recognition of phosphorylated Tau over Tau |
Drosophila melanogaster |
2.7.7.1 |
physiological function |
NMNAT shows strong interaction with phosphorylated truncated Tau protein. The binding affinity of NMNAT3 to phosphorylated Tau is about one order of magnitude higher than that to Tau.The phosphorylated Ser residues of Tau are the primary binding sites. Substrates (i.e. NMN and ATP) and the chaperone client phosphorylated Tau share the same binding pocket with a partial overlap at the phosphate-binding site |
Mus musculus |
2.7.7.18 |
physiological function |
NMNAT serves as a chaperone of phosphorylated Tau to prevent its amyloid aggregation in vitro as well as mitigate its pathology in Drosophila tauopathy models overexpressing human Tau. NMNAT adopts its enzymatic pocket to specifically bind the phosphorylated sites of Tau, which can be competitively disrupted by the enzymatic substrates of NMNAT. NMNAT serves as a cochaperone of Hsp90 for the specific recognition of phosphorylated Tau over Tau |
Drosophila melanogaster |
2.7.7.18 |
physiological function |
NMNAT shows strong interaction with phosphorylated truncated Tau protein. The binding affinity of NMNAT3 to phosphorylated Tau is about one order of magnitude higher than that to Tau.The phosphorylated Ser residues of Tau are the primary binding sites. Substrates (i.e. NMN and ATP) and the chaperone client phosphorylated Tau share the same binding pocket with a partial overlap at the phosphate-binding site |
Mus musculus |