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Literature summary for 2.7.7.1 extracted from

  • Zhai, R.G.; Rizzi, M.; Garavaglia, S.
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme (2009), Cell. Mol. Life Sci., 66, 2805-2818.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Staphylococcus aureus
-
Haemophilus influenzae
-
Escherichia coli
-
Homo sapiens
-
Synechocystis sp.
-
Methanocaldococcus jannaschii
-
Methanothermobacter thermautotrophicus

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
-
-
Escherichia coli
-
-
-
Haemophilus influenzae
-
-
-
Homo sapiens
-
-
-
Methanocaldococcus jannaschii Q57961
-
-
Methanothermobacter thermautotrophicus O26253
-
-
Pseudomonas aeruginosa
-
-
-
Staphylococcus aureus
-
-
-
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Staphylococcus aureus
-
Haemophilus influenzae
-
Escherichia coli
-
Homo sapiens
-
Synechocystis sp.
-
Methanocaldococcus jannaschii
-
Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + nicotinamide ribonucleotide
-
Staphylococcus aureus diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Haemophilus influenzae diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Escherichia coli diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Homo sapiens diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Pseudomonas aeruginosa diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Synechocystis sp. diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Bacillus anthracis diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Methanocaldococcus jannaschii diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide
-
Methanothermobacter thermautotrophicus diphosphate + NAD+
-
r
ATP + nicotinic acid mononucleotide
-
Staphylococcus aureus diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Haemophilus influenzae diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Escherichia coli diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Homo sapiens diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Pseudomonas aeruginosa diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Synechocystis sp. diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Bacillus anthracis diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Methanocaldococcus jannaschii diphosphate + nicotinic acid adenine dinucleotide
-
r
ATP + nicotinic acid mononucleotide
-
Methanothermobacter thermautotrophicus diphosphate + nicotinic acid adenine dinucleotide
-
r

Subunits

Subunits Comment Organism
monomer
-
Escherichia coli
monomer
-
Pseudomonas aeruginosa
oligomer
-
Staphylococcus aureus
oligomer
-
Haemophilus influenzae
oligomer
-
Homo sapiens
oligomer
-
Synechocystis sp.
oligomer
-
Bacillus anthracis
oligomer
-
Methanocaldococcus jannaschii
oligomer
-
Methanothermobacter thermautotrophicus

Synonyms

Synonyms Comment Organism
hNMNAT
-
Homo sapiens
NadM-Nudix
-
Synechocystis sp.
NadR
-
Haemophilus influenzae
NaMNAT
-
Staphylococcus aureus
NaMNAT
-
Escherichia coli
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Staphylococcus aureus
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Haemophilus influenzae
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Escherichia coli
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Homo sapiens
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Pseudomonas aeruginosa
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Synechocystis sp.
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Bacillus anthracis
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Methanocaldococcus jannaschii
nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Methanothermobacter thermautotrophicus
NMNAT
-
Staphylococcus aureus
NMNAT
-
Haemophilus influenzae
NMNAT
-
Escherichia coli
NMNAT
-
Homo sapiens
NMNAT
-
Pseudomonas aeruginosa
NMNAT
-
Synechocystis sp.
NMNAT
-
Bacillus anthracis
NMNAT
-
Methanocaldococcus jannaschii
NMNAT
-
Methanothermobacter thermautotrophicus

General Information

General Information Comment Organism
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Staphylococcus aureus
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Haemophilus influenzae
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Escherichia coli
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Homo sapiens
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Pseudomonas aeruginosa
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Synechocystis sp.
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Bacillus anthracis
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Methanocaldococcus jannaschii
physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Methanothermobacter thermautotrophicus