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
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3.5.1.42
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pyridine
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nicotinic
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nad+
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salvage
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nmnat2
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typhimurium
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phosphoribosyltransferase
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glycohydrolase
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preiss-handler
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adp-ribose
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amidohydrolases
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four-membered
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dyad
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pyrophosphatases
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riboside
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deamidates
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injured
- 3.5.1.42
- pyridine
-
nicotinic
- nad+
-
salvage
- nmnat2
- typhimurium
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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
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3.5.1.42 nicotinamide-nucleotide amidaseAdvanced search results
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results (General Information
General Information on EC 3.5.1.42 - nicotinamide-nucleotide amidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
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recombinant NMN deamidase delays Wallerian degeneration and rescues axonal defects caused by NMNAT2 deficiency in vivo. NMN-consuming activity with axonal NAD-synthesizing enzyme NMNAT2, but not NAD-synthesizing activity, and it delays axon degeneration in primary neuronal cultures. Transgenic NMN deamidase protection is neuron specific and effective against various toxic insults. NMN deamidase prevents NMN accumulation in injured sciatic nerves
additional information
evolution
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the enzyme belongs to the PncC superfamily, active site configuration, structure comparisons, overview
evolution
the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
evolution
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the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
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evolution
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
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metabolism
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the only possible way of nicotinamide salvage in Shewanella oneidensis
metabolism
nicotinamide mononucleotide (NMN) deamidase is one of the key enzymes of the bacterial pyridine nucleotide cycle, PNC
metabolism
the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
metabolism
the hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
metabolism
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the hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
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metabolism
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nicotinamide mononucleotide (NMN) deamidase is one of the key enzymes of the bacterial pyridine nucleotide cycle, PNC
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metabolism
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the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
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metabolism
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the hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
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metabolism
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
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additional information
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enzyme surface charge analysis and substrate docking performed on the enzyme structure from Agrobacterium tumefaciens, PDB code 2A9S, overview
additional information
mutational analysis of AtCinA supports the Ser/Lys catalytic dyad mechanism, overview
additional information
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mutational analysis of AtCinA supports the Ser/Lys catalytic dyad mechanism, overview
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additional information
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mutational analysis of AtCinA supports the Ser/Lys catalytic dyad mechanism, overview
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