3.5.1.42: nicotinamide-nucleotide amidase
This is an abbreviated version!
For detailed information about nicotinamide-nucleotide amidase, go to the full flat file.
Word Map on EC 3.5.1.42
-
3.5.1.42
-
pyridine
-
nicotinic
-
nad+
-
salvage
-
nmnat2
-
typhimurium
-
phosphoribosyltransferase
-
glycohydrolase
-
preiss-handler
-
adp-ribose
-
amidohydrolases
-
four-membered
-
dyad
-
pyrophosphatases
-
riboside
-
deamidates
-
injured
- 3.5.1.42
- pyridine
-
nicotinic
- nad+
-
salvage
- nmnat2
- typhimurium
-
phosphoribosyltransferase
-
glycohydrolase
-
preiss-handler
- adp-ribose
-
amidohydrolases
-
four-membered
-
dyad
- pyrophosphatases
- riboside
-
deamidates
-
injured
Reaction
Synonyms
AtCinA, CinA, nicotinamide mononucleotide amidohydrolase, nicotinamide mononucleotide deamidase, nicotinamide mononucleotide deaminase, nicotinamide nucleoside amidase, Nm deamidase, NMN deamidase, NMN deaminase, OiPncC, PncC, TK1650, YgaD
ECTree
Advanced search results
Subunits
Subunits on EC 3.5.1.42 - nicotinamide-nucleotide amidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
homodimer
oligomer
-
heat-stable and heat-sensitive subunits
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
dimer
-
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
-
dimer
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
-
homodimer
2 * 47320, recombinant His6-tagged enzyme, mass spectrometry
homodimer
-
2 * 47320, recombinant His6-tagged enzyme, mass spectrometry
-