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Information on EC 1.6.1.1 - NAD(P)+ transhydrogenase (Si-specific) and Organism(s) Pseudomonas aeruginosa
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EC Tree 1 Oxidoreductases
1.6 Acting on NADH or NADPH
1.6.1 With NAD+ or NADP+ as acceptor
1.6.1.1 NAD(P)+ transhydrogenase (Si-specific)
IUBMB Comments
The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It is Si-specific with respect to both NAD+ and NADP+. See EC 1.6.1.3, NAD(P)+ transhydrogenase, for enzymes whose stereo specificity is not known.
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.6.1.1
- nadp+
-
transhydrogenation
-
hydride
- rubrum
-
proton-translocating
- rhodospirillum
- succinate
-
submitochondrial
- pntab
-
nadh-binding
-
malic
- beef
-
proton-pumping
- azotobacter
- vinelandii
-
chromatophores
-
energy-dependent
-
substrains
-
energization
-
hymenolepis
- acetylpyridine
-
glutathione-insulin
-
cysteine-free
-
energy-transducing
- n,n'-dicyclohexylcarbodiimide
-
atp-driven
- diminuta
- dccd
- biotechnology
showSynonyms
transhydrogenase, nicotinamide nucleotide transhydrogenase, pyridine nucleotide transhydrogenase, soluble transhydrogenase, soluble pyridine nucleotide transhydrogenase, nad(p) transhydrogenase, non-energy-linked transhydrogenase, nad transhydrogenase, h+-thase, nadph-nad transhydrogenase, more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H+-thase
-
-
-
-
NAD transhydrogenase
-
-
-
-
NAD(P) transhydrogenase
-
-
-
-
NAD(P)(+) transhydrogenase [B-specific]
-
-
-
-
NADH transhydrogenase
-
-
-
-
NADH-NADP-transhydrogenase
-
-
-
-
NADPH-NAD oxidoreductase
-
-
-
-
NADPH-NAD transhydrogenase
-
-
-
-
NADPH:NAD+ transhydrogenase
-
-
-
-
nicotinamide adenine dinucleotide (phosphate) transhydrogenase
-
-
-
-
nicotinamide nucleotide transhydrogenase
-
-
-
-
non-energy-linked transhydrogenase
-
-
-
-
pyridine nucleotide transferase
-
-
-
-
pyridine nucleotide transhydrogenase
-
-
-
-
STH
-
-
-
-
transhydrogenase
-
-
-
-
transhydrogenase, nicotinamide adenine dinucleotide (phosphate)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
NAD(P)/NADPH interconversion
SYSTEMATIC NAME
IUBMB Comments
NADPH:NAD+ oxidoreductase (Si-specific)
The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It is Si-specific with respect to both NAD+ and NADP+. See EC 1.6.1.3, NAD(P)+ transhydrogenase, for enzymes whose stereo specificity is not known.
CAS REGISTRY NUMBER
COMMENTARY
9014-18-0
not distinguished from EC 1.6.1.2
9072-60-0
not distinguished from EC 1.6.1.2
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADPH + 3-acetylpyridine-NAD+
NADP+ + 3-acetylpyridine-NADH
-
Substrates: -
Products: -
Products: -
?
NADPH + deamino-NAD+
NADP+ + deamino-NADH
-
Substrates: -
Products: -
Products: -
?
NADPH + pyridine aldehyde-NAD+
NADP+ + pyridine aldehyde-NADH
-
Substrates: -
Products: -
Products: -
?
NADPH + thio-NADP+ + H+[side 1]
NADP+ + thio-NADPH + H+[side 2]
-
Substrates: -
Products: -
Products: -
?
NADP+ + NADH
NADPH + NAD+
-
Substrates: 4B-specific for NAD(P)H
Products: -
Products: -
?
NADP+ + NADH
NADPH + NAD+
-
Substrates: reduction of NADP+ is preferred
Products: -
Products: -
r
NADP+ + NADH
NADPH + NAD+
-
Substrates: diaphorase-type reactions with NAD(P)H, K3Fe(CN)6 and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
inactivation by heat treatment can be reversed by addition of FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mn2+
-
compared to Ca2+ 10 times higher concetrations are required to obtain the same degree of activation
Ca2+
-
Ca2+-dependent allosteric conformational change, competitive inhibition of activation by Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by palmitoyl-CoA, not affected by treatment with 0.2 mg trypsin/mg protein
-
NADP+
-
0.01 mM, 28% inhibition of NAD+ reduction with NADPH, 12.5% inhibition of NADP+ reduction with NADPH; inhibition of 2'-AMP activated reaction
NADP+
-
inhibition in absence of Ca2+; strong inhibition in the absence of Ca2+, saturation with Ca2+ completely abolishes inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-AMP
-
partially replaceable by 0.3 mM 2',3'-cyclic AMP or coenzyme A
2'-AMP
-
activation of NADP+ reduction by NADH is strongly Ca2+ dependent at nonsaturating concentrations of 2'-AMP
2'-AMP
-
0.5 mM, 26% activation of NAD+ reduction by NADPH, 12.5% activation of NADP+ reduction by NADPH, 1100% activation of NAD+ reduction by NADH, 21% activation of NADP+ reduction by NADH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksUNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A072ZS33_PSEAI
464
0
51161
TrEMBL
Secretory Pathway (Reliability: 3)
A0ABD7K5A4_PSEAI
464
0
51147
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51
-
25 min, 50% inactivation, accelerated by addition of NADPH, reactivation by FAD
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
urea, 8 M, no dissociation, complete inactivation of enzyme activity in 5 M urea
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
urea inactivation: 3% reactivation after dialysis against buffer containing 0.1 mM FAD, 35% after dialysis against buffer containing 1% mercaptoethanol and 95% reactivation after dialysis against buffer containing both 0.1 mM FAD and 1% mercaptoethanol
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Voordouw, G.; van der Vies, S.M.; Themmen, A.P.N.
Why are two different types of pyridine nucleotide transhydrogenase found in living organisms?
Eur. J. Biochem.
131
527-533
1983
Azotobacter vinelandii, Pseudomonas aeruginosa, Pseudomonas fluorescens
Höjeberg, B.; Rydström, J.
Ca2+-dependent allosteric regulation of nicotinamide nucleotide transhydrogenase from Pseudomonas aeruginosa
Eur. J. Biochem.
77
235-241
1977
Pseudomonas aeruginosa
Widmer, F.; Kaplan, N.O.
Regulatory properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa. Kinetic studies and fluorescence titration
Biochemistry
15
4693-4699
1976
Pseudomonas aeruginosa
Wermuth, B.; Kaplan, N.O.
Pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa: purification by affinity chromatography and physicochemical properties
Arch. Biochem. Biophys.
176
136-143
1976
Pseudomonas aeruginosa
Hoek, J.B.; Rydström, J.; Höjeberg, B.
Comparative studies on nicotinamide nucleotide transhydrogenase from different sources
Biochim. Biophys. Acta
333
237-245
1974
Pseudomonas aeruginosa
Rydström, J.; Hoek, J.B.; Höjeberg, B.
Ca 2+ -dependent allosteric regulation of nicotinamide nucleotide transhydrogenase from Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
52
421-429
1973
Pseudomonas aeruginosa
Cohen, P.T.; Kaplan, N.O.
Kinetic characteristics of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa
J. Biol. Chem.
245
4666-4672
1970
Pseudomonas aeruginosa
Cohen, P.T.; Kaplan, N.O.
Purification and properties of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa
J. Biol. Chem.
245
2825-2836
1970
Pseudomonas aeruginosa
Rydström, J.; Hoek, J.B.; Ernster, L.
Nicotinamide nucleotide transhydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
51-88
1976
Pseudomonas fluorescens, Azotobacter vinelandii, Pseudomonas aeruginosa, Azotobacter chroococcum, Azotobacter agilis, Chromatium sp.
-
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