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Enzyme Nomenclature
Information on EC 1.5.1.42 - FMN reductase (NADH)
for references in articles please use BRENDA:EC1.5.1.42
Word Map on EC 1.5.1.42
- 1.5.1.42
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desulfurization
-
bioluminescent
- rhodococcus
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photobacterium
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biodesulfurization
- erythropolis
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fossil
- dibenzothiophene
- phosphoreum
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cost-competitive
- p-hydroxyphenylacetate
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sigma54-dependent
- baumannii
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instantly
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petroleum
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fmnh2-dependent
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.5.1.42
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RECOMMENDED NAME
GeneOntology No.
FMN reductase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
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FMNH2 + NAD+ = FMN + NADH + H+
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-
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FMNH2 + NAD+ = FMN + NADH + H+
catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview
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FMNH2 + NAD+ = FMN + NADH + H+
catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview
Rhodococcus erythropolis IGTS8 / ATCC 53968
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FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD+ oxidoreductase
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
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NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence
physiological function
bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview
physiological function
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Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC
physiological function
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bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview
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physiological function
Rhodococcus erythropolis IGTS8 / ATCC 53968
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Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC
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additional information
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the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
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the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A
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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
FAD + NAD+ + H+
FADH2 + NAD+
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activity with FADH2 and NAD+ is 5% of the activity with FMNH2 and NAD+
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
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-
?
FMN + NADH + H+
FMNH2 + NAD+
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activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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-
?
FMN + NADH + H+
FMNH2 + NAD+
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the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
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-
?
FMN + NADH + H+
FMNH2 + NAD+
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the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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-
?
FMN + NADPH + H+
FMNH2 + NADP+
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activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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-
?
FMN + NADPH + H+
FMNH2 + NADP+
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the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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-
?
additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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-
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additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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-
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additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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additional information
?
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activity with FAD and NADPH is 0.5% of the activity with FMNH2 and NAD+
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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
additional information
?
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P29237
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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additional information
?
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P29237
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
NADH
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activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADPH
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the NADH specific FMN reductase does does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
NADPH
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activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no inhibition by: 0.000325 M dicoumarol, 10 mM KCN, 1% Triton X-100
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additional information
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no inhibition by 0.01 mM 2,4-dinitrophenol, 0.2 mM dicoumarol, 0.1 mM rotenone
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
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0.001
FMN
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pH 5.6, 23°C, spectrometric assay; pH 8.5, 23°C, spectrometric assay
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
purity was too low to permit estimation of specific activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
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bimodal, pH 5: 90% of maximal activity, pH 6.5: about 50% of maximal activity, pH 10: about 70% of maximal activity
5 - 8.6
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the pH curve is bimodal, with maximal activity exhibited at pH 8.6, a minimum at pH 6.0. and a second maximum at pH 5.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
additional information
stopped-flow kinetic experiments are performed at 4°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 43
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effective rate constants of the first and second thermal inactivation stages of coupled enzymes NADH:FMN-oxidoreductase and luciferase in the presence of 1% gelatin, 5% gelatin, or buffer solution (control) at different temperatures, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization in starch and gelatin gels increases the stability of of the enzme to the effects of external conditions
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, in presence of 2 mM dithiothreitol, stable over several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene luxG encoding LuxG, the flavin reductase, is encoded in the same operon as its counterpart LuxAB
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T62A
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the mutant shows 7fold increase in activity compared to the wild type enzyme
T62N
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the mutant shows 5fold increase in activity compared to the wild type enzyme
T62A
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the mutant shows 7fold increase in activity compared to the wild type enzyme
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T62N
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the mutant shows 5fold increase in activity compared to the wild type enzyme
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additional information
additional information
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design of a stable immobilizing reagent for bioluminescent analysis using luciferase, EC 1.14.14., from a recombinant Escherichia coli strain and NADH:FMN-oxidoreductase, EC 1.5.1.42. Natural polymers, gelatin and starch, are used to create a viscous, structured microenvironment for the NADH:FMN-oxidoreductase-luciferase system. Evaluation of the stability of the coupled enzyme system, overview. Both gelatin and starch have a stabilizing effect on the enzymes, the enzymes' activity is increased 2fold in the presence of 1% and 5% of gelatin at 20°C and 25°C, respectively. The acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol/l) is observed, thermal inactivation rate constants of the enzymes at 25-43°C are unchanged
additional information
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the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
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the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.42)
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