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Enzyme Nomenclature
Information on EC 1.5.1.40 - 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
Word Map on EC 1.5.1.40
- 1.5.1.40
-
methanogen
- 8-hydroxy-5-deazaflavins
-
methanococcus
-
hydride
-
hydrogenase
- vannielii
-
methanobacterium
- thermoautotrophicum
-
methanogenesis
- methane
- nicotinamide
-
stereochemical
-
si-face
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
1.5.1.40
-
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RECOMMENDED NAME
GeneOntology No.
8-hydroxy-5-deazaflavin:NADPH oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
reduced coenzyme F420:NADP+ oxidoreductase
The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate [1].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions. The last step of the tetracycline biosynthesis in Streptomyces aureofaciens in which 5a,11a-dehydrochlortetracycline is reduced to chlortetracycline is 8-hydroxy-5-deazaflavin-dependent, and the reducing equivalents are obtained from NADPH
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-O-methyl-7,8-didemethyl-8-hydroxyflavin + NADPH + H+
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
r
5-deaza-8-hydroxyisoalloxazine + NADPH + H+
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate + NADPH + H+
1-deoxy-1-(8-hydroxy-2,4-dioxo-1,3,4,5-tetrahydropyrimido[4,5-b]quinolin-10(2H)-yl)-5-O-phospho-D-ribitol + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
-
the kcat value of the forward reaction is 24 times greater than that of the reverse reaction, thus the production of NADPH at pH 7.0 is more favorable than its consumption
-
-
r
1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
-
the kcat value of the forward reaction is 24 times greater than that of the reverse reaction, thus the production of NADPH at pH 7.0 is more favorable than its consumption
-
-
r
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
-
-
-
-
?
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
-
-
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
-
-
r
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
-
-
?
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
-
-
?
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
-
-
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
direct hydride transfer process, A side-specific, with respect to the prochiral center C5 of the dihydro-8-hydroxy-5-deazaflavin cofactor
-
-
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
of the two substrates NADP+ has to bind first, the binding being associated with an induced fit. The stereochemical analysis of the hydrode transfer leads to the conclusion that the observed orientation of the Si-face of coenzyme F420 towards the Si-face of NADP+ allows only the transfer of the proS hydrogen at C5 to the proS position at C4 and vice versa
-
-
?
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
the enzyme is Si face specific with respect to C5 of reduced coenzyme F420 and Si face specific with respect to C4 of NADP+. The enzyme is specific for both coenzyme F420 and NADP+/NADPH
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
the enzyme exhibits a sequential kinetic mechanism
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
the enzyme exhibits a sequential kinetic mechanism
-
-
r
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions
-
-
?
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
O29370
-
-
-
r
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is not inhibited by iodoacetamide (20 mM), chloromercuribenzoate (20 mM) or N-ethylmaleimide (7 mM) when preincubated for 30 min in the presence of these reagents. The enzyme is not inactivated by dioxygen
-
additional information
inhibitor prediction studies reveal that lovastatin and compactin (mevastatin) produced more affinity for model structure of NADP oxidoreducatse as compared to F420. It indicates that the lovastatin and compactin (mevastatin) compounds (negative regulator) may act as potential inhibitor of F420 dependent NADP oxidoreducatse protein
-
additional information
-
inhibitor prediction studies reveal that lovastatin and compactin (mevastatin) produced more affinity for model structure of NADP oxidoreducatse as compared to F420. It indicates that the lovastatin and compactin (mevastatin) compounds (negative regulator) may act as potential inhibitor of F420 dependent NADP oxidoreducatse protein
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0155
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
0.0625
coenzyme F420
-
pH and temperature not specified in the publication
0.07
NADP+
pH 8.0, temperature not specified in the publication
0.05
NADPH
pH 6.0, temperature not specified in the publication
0.3
oxidized coenzyme F420
pH 6.0, temperature not specified in the publication
0.0077
reduced coenzyme F420
-
pH and temperature not specified in the publication
0.15
reduced coenzyme F420
pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.57
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2295
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
reduction of oxidized coenzyme F420 with NADPH
5.5
7.4
7.9
9.2
pH optimum for reduction of NADP+ with reduced coenzyme F420
5.5
pH optimum for reduction of oxidized coenzyme F420 with NADPH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3 - 6.7
-
pH 4.3: about 50% of maximal activity, pH 6.7: about 50% of maximal activity
4.5 - 6.5
-
pH 4.5: about 45% of maximal activity, pH 6.5: about 35% of maximal activity, reduction of oxidized coenzyme F420 with NADPH
7 - 9
-
pH 7.0: about 60% of maximal activity, pH 9.0: about 50% of maximal activity, reduction of NADP+ with reduced coenzyme F420
7.5 - 10
pH 7.5: about 50% of maximal activity, pH 10.0: about 90% of maximal activity, reduction of NADP+ with reduced coenzyme F420
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
-
15°C: about 45% of maximal activity, 50°C: about 45% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
45000
-
1 * 60000 (alpha) + 1 * 50000 (beta) + 1 * 45000 (gamma), SDS-PAGE
50000
-
1 * 60000 (alpha) + 1 * 50000 (beta) + 1 * 45000 (gamma), SDS-PAGE
60000
-
1 * 60000 (alpha) + 1 * 50000 (beta) + 1 * 45000 (gamma), SDS-PAGE
90000
gradient gel electrophoresis under nondenaturating conditions
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
trimer
homotetramer
4 * 23500, calculated from sequence; 4 * 28000, SDS-PAGE
homotetramer
-
4 * 23500, calculated from sequence; 4 * 28000, SDS-PAGE
-
trimer
-
1 * 60000 (alpha) + 1 * 50000 (beta) + 1 * 45000 (gamma), SDS-PAGE
trimer
-
1 * 60000 (alpha) + 1 * 50000 (beta) + 1 * 45000 (gamma), SDS-PAGE
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, crystal structure of the enzyme bound with coenzyme F420. The structure resolved to 1.65 A contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 A, which is optimal for hydride transfer
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in 0.08 M NaCl a half-life of 9 h is found which increased to greater than 6000 h in 1 M NaCl (both in the presence of 2% ethylene glycol)
-
neither high salt or protease inhibitors were effective in stabilizing the activity of the partially purified enzyme
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethylene glycol
-
enhanced the stability: half-life increased from 9 to 750 h in 18% ethylene glycol (in 0.08 M NaCl)
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-75°C, 2 months, at low concentration (0.066 mg/ml), in the presence of ethylene glycol, 20% (v/v), no loss of activity
-
4°C, at low concentration (0.066 mg/ml), in the presence of ethylene glycol, 20% (v/v), 22% of the activity is lost
-
4°C, at low concentration (0.066 mg/ml), the purified enzyme loses 84% of its activity in 2 days
-
4°C, purified enzyme at a protein concentration of 20 mg/ml is completely stable when stored at 4°C in 50 mM Tricine/KOH pH 8.0 containing 0.2 M KCl
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.40)
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