2.7.1.180: FAD:protein FMN transferase
This is an abbreviated version!
For detailed information about FAD:protein FMN transferase, go to the full flat file.
Word Map on EC 2.7.1.180
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2.7.1.180
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flavinylation
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vibrio
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flavoproteins
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na+-translocating
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nadh:quinone
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phosphoester
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mononucleotide
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fumarate
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cholerae
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klebsiella
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pneumoniae
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na+-nqr
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harveyi
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fluorogenic
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proteobacteria
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prosthetic
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pallidum
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fmn-binding
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redox-active
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metal-dependent
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spirochete
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syphilis
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isoalloxazine
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pyrophosphatase
- 2.7.1.180
-
flavinylation
- vibrio
- flavoproteins
-
na+-translocating
-
nadh:quinone
-
phosphoester
- mononucleotide
- fumarate
- cholerae
-
klebsiella
- pneumoniae
- na+-nqr
- harveyi
-
fluorogenic
- proteobacteria
-
prosthetic
- pallidum
-
fmn-binding
-
redox-active
-
metal-dependent
-
spirochete
-
syphilis
- isoalloxazine
- pyrophosphatase
Reaction
Synonyms
AbpE, apbE, ApbE1, ApbE2, apbE_2, FAD:threonine flavin transferases, flavin transferase, flavin-trafficking protein, FMN transferase, FRD, frd-apbE, Ftp, Ftp_Ec, Mg2+-dependent FAD:protein FMN transferase, Mg2+-dependent FMN transferase, More, protein-dependent FMN transferase
ECTree
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KM Value
KM Value on EC 2.7.1.180 - FAD:protein FMN transferase
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0.1
[Vibrio cholerae protein NqrC]-L-threonine
above, pH 9.0, 22°C, recombinant wild-type enzyme
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0.0001
FAD
pH 9.0, temperature not specified in the publication, wild-type enzyme
0.00019
FAD
pH 9.0, temperature not specified in the publication, mutant H257t
0.0002
FAD
pH 9.0, temperature not specified in the publication, mutant H257G
0.011
pH 9.0, temperature not specified in the publication, wild-type enzyme
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0.087
[protein NqrC]-L-threonine
pH 9.0, temperature not specified in the publication, mutant H257G
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0.119
[protein NqrC]-L-threonine
pH 9.0, temperature not specified in the publication, mutant H257t
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additional information
ApbE activity is highly sensitive to FAD, and is saturated at 0.001 mM
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additional information
additional information
ApbE follows a random Bi Bi sequential kinetic mechanism, in which a ternary complex is formed, indicating that both substrates must be bound to the enzyme for the reaction to proceed, Michaelis-Menten steady-state kinetic analysis, kinetic mechanism
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additional information
additional information
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ApbE follows a random Bi Bi sequential kinetic mechanism, in which a ternary complex is formed, indicating that both substrates must be bound to the enzyme for the reaction to proceed, Michaelis-Menten steady-state kinetic analysis, kinetic mechanism
-
additional information
additional information
single-turnover kinetics
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