Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.5.1 - NAD+ synthase (glutamine-hydrolysing) and Organism(s) Homo sapiens and UniProt Accession Q6IA69

for references in articles please use BRENDA:EC6.3.5.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q6IA69
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
nade1, nitrogen-regulatory protein, glutamine-dependent nad synthetase, mtunade, glutamine-dependent nad+ synthetase, gsp38, glutamine-dependent nadegln, nicotinamide adenine dinucleotide synthetase enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
General stress protein 38
-
-
-
-
GSP38
-
-
-
-
NAD synthetase (glutamine)
-
-
-
-
NAD(+) synthase [glutamine-hydrolyzing]
-
-
-
-
NAD+ synthetase (glutamine-hydrolysing)
-
-
-
-
Nicotinamide adenine dinucleotide synthetase (glutamine)
-
-
-
-
Nitrogen-regulatory protein
-
-
-
-
Sporulation protein outB
-
-
-
-
Synthetase, nicotinamide adenine dinucleotide (glutamine)
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
deamido-NAD+:L-glutamine amido-ligase (AMP-forming)
NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
37318-70-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
show the reaction diagram
-
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
show the reaction diagram
NADsyn1 uses not only ammonia but also glutamine. The Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
show the reaction diagram
NADsyn1 uses not only ammonia but also glutamine. The Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
-
-
?
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
gossypol
-
-
Pb2+
-
-
Zn2+
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.154
ATP
0.04 - 0.2
deamido-NAD+
2.17
Gln
-
-
0.001
L-Gln
-
pH 7.5
1.44
L-glutamine
37°C, wild-type NADsyn1
13.1 - 23.9
NH3
64.2
NH4+
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.017
-
-
additional information
-
coupled enzyme assay for the measurement of recombinant human NAD+ synthetase by employing lactate dehydrogenase in a cycling/amplification reaction linked ultimately to the fluorescence generation of resorufin from reazurin via diaphorase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.4
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
6.0: about 75% of maximal activity, 8.0: about 55% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NADE_HUMAN
706
0
79285
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
483000
-
gel filtration
500000
non-denaturing PAGE
80000
6 * 80000, wild-type and C175S mutant enzyme, SDS-PAGE
80300
6 * 80300, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C175S
in contrast with the wild-type NADsyn1, the activity of the mutant NADsyn1 (C175S-NADsyn1) is not detected when glutamine is used as a substrate, whereas the activity remains unaltered with NH4Cl
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA and KCl increase stability substantially
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 24 h, complete loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 insect cells
-
expression of Nadsyn1 and mutant enzyme C175S as His6-tagged proteins in COS-7 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
erythrocyte NAD synthetase is activated by lead, and the activity is a sensitive indicator of lead exposure in human
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zerez, C.R.; Wong, M.D.; Tanaka, K.R.
Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure
Blood
75
1576-1582
1990
Homo sapiens
Manually annotated by BRENDA team
Hara, N.; Yamada, K.; Terashima, M.; Osago, H.; Shimoyama, M.; Tsuchiya, M.
Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency
J. Biol. Chem.
278
10914-10921
2003
Homo sapiens (Q6IA69), Homo sapiens
Manually annotated by BRENDA team
Bembenek, M.E.; Kuhn, E.; Mallender, W.D.; Pullen, L.; Li, P.; Parsons, T.
A fluorescence-based coupling reaction for monitoring the activity of recombinant human NAD synthetase
Assay Drug Dev. Technol.
3
533-541
2005
Homo sapiens
Manually annotated by BRENDA team