Information on EC 2.7.7.2 - FAD synthetase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.7.7.2
-
RECOMMENDED NAME
GeneOntology No.
FAD synthetase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + FMN = diphosphate + FAD
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
nucleotidyl group transfer
Q8VZR0, Q9FMW8
;
PATHWAY
KEGG Link
MetaCyc Link
flavin biosynthesis I (bacteria and plants)
-
flavin biosynthesis II (archaea)
-
flavin biosynthesis III (fungi)
-
flavin biosynthesis IV (mammalian)
-
Metabolic pathways
-
Riboflavin metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:FMN adenylyltransferase
Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [3]. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosine triphosphate-riboflavin mononucleotide transadenylase
-
-
-
-
adenosine triphosphate-riboflavine mononucleotide transadenylase
-
-
-
-
ATP-FMN adenylyltransferase
-
-
ATP:FMN adenylyl transferase
-
-
ATP:FMN adenylyltransferase
-
-
AtRibF1
Q9FMW8
-
AtRibF2
Q8VZR0
-
FAD pyrophosphorylase
-
-
-
-
FAD synthetase
Q8VZR0, Q9FMW8
-
FAD synthetase
-
bifunctional enzyme: riboflavin kinase
FAD synthetase
Q8NFF5
-
FAD synthetase
-
-
FAD synthetase isoform 1
-
-
FAD synthetase isoform 2
-
-
FAD synthetase isoform 2
Q8NFF5
-
FADS1
Q8NFF5
-
FADS2
Q8NFF5
-
FADS2
Q8NFF5
isoform
flavin adenine dinucleotide synthetase
-
-
FMN adenylyltransferase
-
-
-
-
FMN adenylyltransferase
Q6FNA9
-
FMN pyrophosporylase
-
-
-
-
riboflavin adenine dinucleotide pyrophosphorylase
-
-
-
-
riboflavin mononucleotide adenylyltransferase
-
-
-
-
riboflavine adenine dinucleotide adenylyltransferase
-
-
-
-
MJ1179
Q58579
gene name
additional information
-
bifunctional enzyme with EC 2.7.1.26 and EC 2.7.7.2 activity
additional information
Thermotoga maritima TM379
-
bifunctional enzyme with EC 2.7.1.26 and EC 2.7.7.2 activity
-
CAS REGISTRY NUMBER
COMMENTARY
9026-37-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform RibF1
UniProt
Manually annotated by BRENDA team
This UniProt-ID has been deleted; isoform RibF1
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 1012
1012
Uniprot
Manually annotated by BRENDA team
ATCC6872 and KY13315, previously Brevibacterium ammoniagenes
-
-
Manually annotated by BRENDA team
bifunctional enzyme, displays activities of EC 2.7.7.2 and EC 2.7.1.26
SwissProt
Manually annotated by BRENDA team
FAD synthetase gene nucleotide sequence
SwissProt
Manually annotated by BRENDA team
Corynebacterium ammoniagenes ATCC6872
ATCC6872
-
-
Manually annotated by BRENDA team
; isoform Fads2
SwissProt
Manually annotated by BRENDA team
cv. Bright Yellow 2
-
-
Manually annotated by BRENDA team
baker's yeast, brewers' yeast, beer yeast
-
-
Manually annotated by BRENDA team
baker's yeast, brewers' yeast, beer yeast, FAD1 nucleotide sequence
SwissProt
Manually annotated by BRENDA team
bifunctional flavokinase/flavin adenine dinucleotide synthetase
-
-
Manually annotated by BRENDA team
strain TM379
-
-
Manually annotated by BRENDA team
Thermotoga maritima TM379
strain TM379
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4'-butyl-FMN
diphosphate + 4'-butylflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 5'-pentyl-FMN
diphosphate + 5'-pentylflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 7,8-dibromo-FMN
diphosphate + 7,8-dibromoflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 7,8-dichloro-FMN
diphosphate + 7,8-dichloroflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 7-chloro-FMN
diphosphate + 7-chloroflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 8-chloro-FMN
diphosphate + 8-chloroflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, P54575
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
P38913, -
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, Q59263
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, Q59263
-
-
-
ATP + FMN
diphosphate + FAD
show the reaction diagram
Q59263
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
P38913
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, Q8NFF5
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
Q8NFF5
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, Q0WS47, Q9FMW8
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
Q8VZR0, Q9FMW8
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
essentially irreversible in the direction of FAD formation
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
adenylation of FMN is reversible, FAD and diphosphate can be converted to FMN and ATP by the enzyme, under the conditions studied phosphorylation of riboflavin is irreversible
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
-
-
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, P54575
essential for flavin metabolism
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, Q58579
the enzyme does not catalyze the reverse reaction to produce FMN and ATP from FAD and diphosphate
-
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
Corynebacterium ammoniagenes ATCC6872
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
Thermotoga maritima TM379
-
-
-
-
?
ATP + iso-FMN
diphosphate + isoflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
?
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
?
show the reaction diagram
-
-
-
-
ir
ATP + roseoflavin mononucleotide
diphosphate + roseoflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
CTP + FMN
diphosphate + flavin cytidine dinucleotide
show the reaction diagram
-, Q58579
-
-
-
?
diphosphate + FAD
ATP + FMN
show the reaction diagram
-
-
-
r
diphosphate + FAD
ATP + FMN
show the reaction diagram
-
-
-
r
diphosphate + FAD
ATP + FMN
show the reaction diagram
-
-
-
-
r
diphosphate + FAD
ATP + FMN
show the reaction diagram
-
low reaction rate
-
-
r
FMN + ATP
FAD + diphosphate
show the reaction diagram
-
-
-
-
?
FMN + ATP
FAD + diphosphate
show the reaction diagram
-
-
-
-
?
FMN + ATP
FAD + diphosphate
show the reaction diagram
-, Q6FNA9
-
-
-
?
GTP + FMN
diphosphate + flavin guanidine dinucleotide
show the reaction diagram
-, Q58579
weak specific activity
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
in the reverse reaction diphosphate cannot be replaced by orthophosphate or metaphosphate
-
-
-
additional information
?
-
-
if the hydrogen-bonding capacity of the NH group at position 3 is blocked or removed by substitution, FMN analogues do not act as substrates or inhibitors, 3-deaza-FMN, 7,8-didemethyl-8-hydroxy-5-deaza-FMN, 5-methyl-7,8-didemethyl-8-hydroxy-5-deaza-(5-methyl)-FMN, 5'-sulfate-FMN, 5'-deoxy-FMN, 10-(3-chlorobenzyl)-FMN and 10-(hydroxyethyl)-5-deaza-FMN are no substrates
-
-
-
additional information
?
-
-, P54575
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
Q59263
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-, P54575
highly purified 5'-FMN is not accepted as a substrate
-
-
-
additional information
?
-
-
does not use 8-demethyl-8-amino-riboflavin mononucleotide as substrate
-
-
-
additional information
?
-
-
FAD synthetase presents two catalytic modules, a C-terminus with ATP-riboflavin kinase activity and an N-terminus with ATP-flavin mononucleotide adenylyltransferase activity
-
-
-
additional information
?
-
-, Q58579
the enzyme does not function as a glycerol-3-phosphate cytidylyltransferase because it fails to catalyze the formation of glycerol cytidine dinucleotide when incubated with DL-glycerol 3-phosphate and CTP
-
-
-
additional information
?
-
Corynebacterium ammoniagenes ATCC6872
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
P38913, -
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, Q59263
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
Q8VZR0, Q9FMW8
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
-
-
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
-
ir
ATP + FMN
diphosphate + FAD
show the reaction diagram
-, P54575
essential for flavin metabolism
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
-
catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
Corynebacterium ammoniagenes ATCC6872
-
-
-
r
ATP + FMN
diphosphate + FAD
show the reaction diagram
Thermotoga maritima TM379
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
no FAD synthesis in absence of ATP, ADP cannot replace ATP
ATP
-
nucleoside triphosphates other than ATP do not act as substrates or inhibitors
flavin
-, Q59263
presence of a flavin binding site for the adenylylation activity, independent from that related with the phosphorylation actiity
FMN
Q8VZR0, Q9FMW8
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
about 30% of the activity with Mg2+
Ca2+
-
Ca2+ gives maximum FAD synthesis equal to 62% of that measured with Mg2+
Co2+
-
effective for FMN production
Co2+
-, Q58579
the enzyme requires divalent metals for activity, the best activity being observed with Co2+, where the activity is 4times greater than that with Mg2+
Co2+
-
in the presence of about 0.5 mM Co2+, the activity is almost equal to that measured with Mg2+
Cu2+
-
effective for FMN production
Fe2+
-, Q58579
the enzyme contains 0.2 mol of iron per protomer
Mg2+
-
required for FAD synthesis, optimal concentration 1.5 mM, inhibition at higher levels
Mg2+
-
-
Mg2+
-
strict requirement for MgCl2
Mg2+
-, Q6FNA9
-
Mg2+
-, Q58579
low stimulation of activity; the enzyme contains 8.4 mol of magnesium per protomer
Mg2+
-
MgCl2 is strictly required for both the synthetic and diphosphorolytic activity, FAD synthesis is abolished in the absence of MgCl2
MgCl2
Q8NFF5
strictly required
Mn2+
-
about 15% of the activity with Mg2+
Mn2+
-, Q58579
the activity with Mn2+ is 4times lower than that with Co2+
Ni2+
-, Q58579
weak stimulation of activity
Zn2+
-
effective for FMN production
Mn2+
-
Mn2+ gives maximum FAD synthesis equal to 77% of that measured with Mg2+
additional information
-
Zn2+ cannot replace Mg2+
additional information
-
Ba2+, Co2+, Cu2+, Cd2+, Fe2+, Ni2+, Sn2+ and Sr2+ do not show any activity; Zn2+ cannot replace Mg2+
additional information
-
not basically effected by Mg2+, FAD production slightly inhibited at high concentrations
additional information
-, Q58579
the enzyme activity is not stimulated by Zn2+ and Fe2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,5-Dideaza-FMN
-
-
5'-sulfo-FMN
-
-
8-Hydroxy-7-methyl-FMN
-
-
ATP
-
inhibits FAD cleavage completely
ATP
-
substrate inhibition; substrate inhibition
D-glucose 6-phosphate
-
-
D-lyxose 5-phosphate
-
-
diphosphate
-
product inhibition
FAD
-
strong product inhibitor, 50% inhibition at 0.006 mM, competitive inhibition against ATP, mixed inhibition against FMN
FMN
-
substrate inhibition
FMN
-
70% inhibited when using FMN concentrations higher than 0.004 mM
FMN
-
substrate inhibition; substrate inhibition
FMN
-
90% inhibition at 0.01 mM
GDP
-
competitive inhibition
GTP
-
uncompetitive inhibition
NAD+
-
inhibits FAD cleavage completely
Riboflavin 5'-diphosphate
-
weak cofactor for FAD-requiring enzymes
Urea
-
the enzymatic activity of isoform FADS2 decreases dramatically at increasing urea concentration, with a mid-point for activity loss at 2.1 m urea
Zn2+
-
1 mM inhibits activity by 60%
Zn2+
-
specific inhibition of adenylyltransferase activity
hexyl 6-phosphate
-
-
additional information
-
no detectable inhibition with 2-[(hydroxyethyl)amino]-FMN, 2-morpholinyl-FMN, 2-(phenylamino)-FMN, 3-methyl-FMN, 3-(carboxymethyl)-FMN, 8-alpha-imidazolyl-FMN, 8-alpha-(N-methylimidazolyl)-FMN, 5'-phosphothionate, DL-glycerol 3-phosphate and propyl 3-phosphate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-, Q58579
the enzyme reaches its maximal activity at an ATP concentration of about 1.4 mM. The enzyme activity decreases by 20% when the concentration of ATP is higher than the physiologically relevant concentration (about 5 mM)
CTP
-, Q58579
the activity of the enzyme reaches its maximal activity at a CTP concentration of about 1.4 mM. The maximal activity decreases by 68 and 95% when the concentration of CTP is 5.7 and 11.4 mM, respectively
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.25
-
4'-butyl-FMN
-
pH 7.1, 37C
0.0048
-
7,8-dibromo-FMN
-
pH 7.1, 37C, direct assay
0.94
-
7,8-dibromo-FMN
-
pH 7.1, 37C, indirect assay
0.082
-
7,8-dichloro-FMN
-
pH 7.1, 37C, indirect assay
0.12
-
7,8-dichloro-FMN
-
pH 7.1, 37C, direct assay
0.0076
-
7-chloro-FMN
-
pH 7.1, 37C, indirect assay
0.0086
-
7-chloro-FMN
-
pH 7.1, 37C, direct assay
0.019
-
8-chloro-FMN
-
pH 7.1, 37C
0.0107
-
ATP
-, Q6FNA9
-
0.0111
-
ATP
Q0WS47, Q9FMW8
pH 8.5
0.0111
-
ATP
Q8VZR0, Q9FMW8
at pH 8.5
0.0131
-
ATP
Q0WS47, Q9FMW8
pH 8.5
0.0131
-
ATP
Q8VZR0, Q9FMW8
at pH 8.5
0.0153
-
ATP
-
at 37C, in 50 mM Tris-HCl, pH 7.5
0.025
-
ATP
-, Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.03568
-
ATP
-
wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.037
-
ATP
-
pH 7.6, 25C
0.0382
-
ATP
-
mutant enzyme T208D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0387
-
ATP
-
mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0435
-
ATP
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
0.04537
-
ATP
-
mutant enzyme T208A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.04647
-
ATP
-
mutant enzyme E268A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.04704
-
ATP
-
mutant enzyme N210A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.053
-
ATP
-
pH 7.5, 37C
0.071
-
ATP
-
pH 8.0, 37C, MgATP
0.07667
-
ATP
-
mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.079
-
ATP
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
0.48
-
CTP
-, Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.114
-
diphosphate
-
pH 7.6, 25C
0.0004
-
FAD
-
pH 7.6, 25C
0.00035
-
FMN
-
at 37C, in 50 mM Tris-HCl, pH 7.5
0.00036
-
FMN
Q8NFF5
at 37C
0.00036
-
FMN
-
-
0.0004
-
FMN
Q8NFF5
37C
0.00076
-
FMN
-, Q6FNA9
-
0.00088
-
FMN
-
mutant enzyme E268A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2; mutant enzyme T208D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00095
-
FMN
-
mutant enzyme T208A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.001
-
FMN
-
pH 7.6, 25C
0.00117
-
FMN
-
mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00119
-
FMN
-
wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0013
-
FMN
-
-
0.0054
-
FMN
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
0.0079
-
FMN
-
pH 7.1, 37C, indirect assay
0.00823
-
FMN
-
mutant enzyme N210A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0091
-
FMN
-
pH 8.0, 37C
0.0094
-
FMN
-
pH 7.5, 37C
0.0094
-
FMN
-
pH 7.1, 37C
0.0095
-
FMN
-
pH 7.1, 37C, direct assay
0.01501
-
FMN
-
mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0189
-
FMN
Q0WS47, Q9FMW8
pH 8.5
0.0189
-
FMN
Q8VZR0, Q9FMW8
at pH 8.5
0.0208
-
FMN
Q0WS47, Q9FMW8
pH 8.5
0.0208
-
FMN
Q8VZR0, Q9FMW8
at pH 8.5
0.0311
-
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
0.055
-
FMN
-
-
0.063
-
FMN
-, Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.068
-
FMN
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
0.109
-
FMN
-
without Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
1.5
-
FMN
-
at 37C
0.116
-
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
-
0.015
-
iso-FMN
-
pH 7.1, 37C
additional information
-
additional information
-, Q6FNA9
R297A mutant protein: increased apparent KM-values for ATP and FMN by about 5 and 3times, respectively, compared to the wild-type enzyme
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0107
-
ATP
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.011
-
ATP
Q0WS47, Q9FMW8
pH 8.5
0.0128
-
ATP
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.013
-
ATP
Q0WS47, Q9FMW8
pH 8.5
0.087
-
ATP
-, Q6FNA9
-
0.000075
-
FAD
-
pH 7.6, 25C
0.0000833
-
FMN
-
pH 7.6, 25C
0.0036
-
FMN
Q8NFF5
37C; at 37C
0.0036
-
FMN
-
-
0.0048
-
FMN
-
-
0.0108
-
FMN
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.011
-
FMN
Q0WS47, Q9FMW8
pH 8.5
0.0128
-
FMN
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.013
-
FMN
Q0WS47, Q9FMW8
pH 8.5
0.02
-
FMN
-
without Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
0.047
-
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
0.078
-
FMN
-
at 37C, in 50 mM Tris-HCl, pH 7.5
0.08
-
FMN
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
0.087
-
FMN
-, Q6FNA9
-
0.33
-
FMN
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
0.07
-
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.16
-
ATP
-, Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
22040
1.1
-
ATP
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
22040
3.8
-
ATP
-
mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
4.2
-
ATP
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
22040
4.3
-
ATP
-
mutant enzyme N210A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
7.3
-
ATP
-
mutant enzyme E268A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
7.7
-
ATP
-
mutant enzyme T208A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
8
-
ATP
-
wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
8.2
-
ATP
-
mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
8.5
-
ATP
-
mutant enzyme T208D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
22040
0.006
-
CTP
-, Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
8829
0.0311
-
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
10560
0.064
-
FMN
-, Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
10560
0.83
-
FMN
-
without Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
10560
1.2
-
FMN
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
10560
19.7
-
FMN
-
mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
24.8
-
FMN
-
mutant enzyme N210A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
61.7
-
FMN
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37C
10560
238.3
-
FMN
-
wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
270.2
-
FMN
-
mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
365.7
-
FMN
-
mutant enzyme T208D, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
369.2
-
FMN
-
mutant enzyme T208A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
386
-
FMN
-
mutant enzyme E268A, at 37C in 20 mM PIPES pH 7.0, 10 mM MgCl2
10560
0.6
-
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37C
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.029
-
1,5-Dideaza-FMN
-
pH 7.1, 37C
0.283
-
1-Deaza-FMN
-
pH 7.1, 37C
0.106
-
2-thio-FMN
-
pH 7.1, 37C
0.291
-
5'-sulfo-FMN
-
pH 7.1, 37C
0.002
-
8-Hydroxy-7-methyl-FMN
-
pH 7.1, 37C
0.013
-
ATP
Q0WS47, Q9FMW8
pH 8.5
0.01302
-
ATP
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.01868
-
ATP
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.0187
-
ATP
Q0WS47, Q9FMW8
pH 8.5
31
-
ATP
-, Q58579
in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.019
-
D-glucose 6-phosphate
-
pH 7.1, 37C
0.184
-
D-lyxose 5-phosphate
-
pH 7.1, 37C
0.00064
-
diphosphate
-
pH 7.6, 25C
0.06
-
diphosphate
-
pH 7.6, 25C
0.066
-
diphosphate
-
pH 8.0, 37C, against FMN
0.00075
-
FAD
-
pH 8.0, 37C, against FMN
0.0013
-
FAD
-
pH 8.0, 37C, against MgATP 2-
0.00085
-
FMN
Q0WS47, Q9FMW8
pH 8.5
0.00085
-
FMN
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
0.00092
-
FMN
Q0WS47, Q9FMW8
pH 8.5
0.00092
-
FMN
Q8VZR0, Q9FMW8
recombinant enzyme purified under native conditions, at pH 8.5
2.5
-
GDP
-
at 37C, in 50 mM Tris-HCl, pH 7.5
1.8
-
GTP
-
at 37C, in 50 mM Tris-HCl, pH 7.5
0.009
-
Riboflavin 5'-diphosphate
-
-
0.266
-
hexyl 6'-phosphate
-
pH 7.1, 37C
additional information
-
additional information
-
Ki value for diphosphate against ATP not determined because Lineweaver-Burk plots of inhibition by diphosphate with varying concentrations of ATP are nonlinear
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001
-
-, Q58579
using GTP as cosubstrate, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.0039
-
-
-
0.004
-
-, Q58579
using CTP as cosubstrate, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.0044
-
-
-
0.01
-
-, Q58579
using ATP as cosubstrate, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70C
0.03
-
Q8NFF5
at 37C
0.58
-
P54575
-
0.59
-
-
crude cell extract, at 37C
6.8
-
-
after 12.5fold purification, at 37C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.1
-
-
-
7
7.4
-
FMN used as substrate
7.8
8
-
riboflavin used as substrate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
37
-
riboflavin used as substrate
37
40
-
FMN used as substrate
60
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.66
-
-
isoelectric focusing
6
-
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q0WS47, Q9FMW8
mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA; mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
Manually annotated by BRENDA team
Q8VZR0, Q9FMW8
;
Manually annotated by BRENDA team
Q0WS47, Q9FMW8
mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA; mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
Manually annotated by BRENDA team
additional information
Q0WS47, Q9FMW8
relative expression levels show little or no variation among the organs and at the developmental stages examined. Exceptions are mature siliques and germinated seeds, which expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA; relative expression levels show little or no variation among the organs and at the developmental stages examined. Exceptions are mature siliques and germinated seeds, which expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
Manually annotated by BRENDA team
additional information
Q8VZR0, Q9FMW8
expression levels of AtRibF1 show little or no variation among the organs and at the developmental stages examined, 2 exceptions are mature siliques and germinated seeds, which express 50-100% more AtRibF1 mRNA, AtRibF1 is a housekeeping enzyme needed by all plant organs throughout development; expression levels of AtRibF2 show little or no variation among the organs and at the developmental stages examined, AtRibF2 are housekeeping enzyme needed by all plant organs throughout development
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
P38913, -
presence of mitochondrial FAD synthetase activity in strains transformed with FAD1 on a high-copy-number plasmid, but not in mitochondria of wild-type strains
Manually annotated by BRENDA team
-
membrane-enriched fraction
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28800
-
Q0WS47, Q9FMW8
gel filtration
28800
-
Q8VZR0, Q9FMW8
estimated by gel filtration
29000
-
-, Q58579
gel filtration
29200
-
Q0WS47, Q9FMW8
gel filtration
29200
-
Q8VZR0, Q9FMW8
estimated by gel filtration
34180
-
P54575
wild-type, gel filtration
34200
-
P54575
gel filtration, nondenaturing conditions
34230
-
P54575
mutant RibC, gel filtration
35670
-
P54575
deduced from RibC open reading frame; mass spectroscopy
36000
-
P54575
wild-type, SDS-PAGE
36000
-
P38913, -
recombinant enzyme, expressed in E. coli, PAGE; recombinant enzyme, expressed in E. coli, PAGE
37120
-
-
electrospray mass spectrometry, Se-Met-enzyme, 36843.5 is the theoretical value for the native protein
37710
-
-, Q59263
deduced from amino acid sequence
38000
-
-, Q59263
SDS-PAGE
54190
-
-
calculated from amino acid sequence
55000
-
Q8NFF5
SDS-PAGE, T7-tagged enzyme
55840
-
Q8NFF5
calculated from amino acid sequence, T7-tagged enzyme
60000
-
-
SDS-PAGE, isoform 2
63000
-
-
SDS-PAGE
65270
-
-
calculated from amino acid sequence
97000
-
-
gel filtration
140000
-
-
gel filtration, purified enzyme can be separated into low molecular weight component of MW 140000 and MW 325000 high molecular weight component
325000
-
-
gel filtration, purified enzyme can be separated into low molecular weight component of MW 140000 and high molecular weight component of MW325000
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q8NFF5
x * 55000, SDS-PAGE, x * 55844, calculated
?
-
x * 34000, His-tagged recombinant protein, SDS-PAGE
?
-
x * 54200 Da, predicted; x * 65300 Da, predicted
?
Q59263
x * 38000, estimated from amino acid sequence; x * 40000-41000, SDS-PAGE
?
-
x * 56537, isoform FADS2, calculated from amino acid sequence; x * 57000, isoform FADS2, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
crystal structure analysis
dimer
Thermotoga maritima TM379
-
crystal structure analysis
-
hexamer
-
x-ray crystallography
homodimer
-, Q58579
2 * 17000, SDS-PAGE
monomer
P54575
1 * 36000, SDS-PAGE
monomer
-, Q59263
1 * 38000, SDS-PAGE
monomer
Q0WS47, Q9FMW8
1 * 33900, SDS-PAGE and calculated; 1 * 34200, SDS-PAGE and calculated
monomer
Q8VZR0, Q9FMW8
estimated by gel filtration; estimated by gel filtration
monomer
-, Q6FNA9
crystal structure, gel filtration
monomer
Corynebacterium ammoniagenes ATCC6872
-
1 * 38000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3D structural model for based on the structure of Thermotoga maritima FADS
-, Q59263
hanging-drop vapor-diffusion method, 277 K
-
mutant enzyme E268D, hanging drop vapor diffusion method
-
in complex with FAD, hanging drop vapor diffusion method
P38913
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.4
-
at pH 6.0 10% as active as at pH 7.5, at pH 8.4 64%
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
enzyme denatured as temperature increases, completely inactivated above, bovine serum albumin stabilizes up to 45C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
thiol maintains stability
-
thiols protects the activity, can partly restore inactivated enzyme
-
purified enzyme is instable
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
aerobically isolated enzyme is active only under reducing conditions (with 5.6 mM dithiothreitol)
-, Q58579
721625
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 2 weeks
P54575
-20C, 1 mM dithiothreitol, 20% glycerol can be stored without significant loss of activity for 1 week
-
4C, activity largely lost within 1 week
-
5C, if dithiothreitol is removed from the purified enzyme solution enzyme denatures within 12 h
-
3C, loses 20-30% of its activity in 4 days, 58% in 11 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by ion exchange chromatography and gel filtration; by Ni-NTA affinity chromatography, ion exchange chromatography and gel filtration
Q8VZR0, Q9FMW8
recombinant protein; recombinant protein
Q0WS47, Q9FMW8
wild-type and recombinant enzyme
P54575
Ni-Sepharose affinity chromatography, anion exchange chromatography, hydrophobic interaction chromatography, gel filtration
-, Q6FNA9
ammonium sulfate fractionation, Phenyl-Sepharose chromatography, DEAE-Cellulose chromatography
-
DEAE-cellulose column chromatography, phenyl Sepharose column chromatography, and Sephacryl S-200 gel filtration
Q59263
phenyl Sepharose column chromatography and DEAE-cellulose column chromatography
-
; recombinant protein
Q8NFF5
Ni2+-chelating column chromatography and hydroxyapatite column chromatography
-
Ni2+-chelating Sepharose Fast Flow column chromatography
-
Ni2+-nitrilotriacetic-agarose column chromatography
-
Mono Q column chromatography
-, Q58579
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned in Escherichia coli; cloned in Escherichia coli
Q8VZR0, Q9FMW8
expression in Escherichia coli; expression in Escherichia coli
Q0WS47, Q9FMW8
ribC encodes a bifunctional flavokinase/FAD-synthetase, cloned and overexpressed in Escherichia coli BL21
P54575
His-tagged version expressed in Escherichia coli BL21(DE3)
-, Q6FNA9
; FAD synthetase gene cloned and overexpressed in Escherichia coli JM105
-, Q59263
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3), a SeMet-version is generated
-
expressed in Escherichia coli BL21(DE3) cells
Q59263
expression in Escherichia coli
-, Q59263
FAD synthetase overproducing recombinant Corynebacterium ammoniagenes KY13315 constructed from ATCC6872, gene cannot be expressed in Escherichia coli
-
vector pET-23a(+) cloned and overexpressed in Escherichia coli JM109(DE-3)
-
expressed in Escherichia coli strain Rosetta(DE3)
-
expressed in Escherichia coli strain Rosetta(DE3); expression in Escherichia coli
Q8NFF5
expressed in Escherichia coli strains BL21 and Rosetta (DE3) and in Pichia pastoris strain X33
-
expressed in Escherichia coli; expressed in Escherichia coli, in BHK-21 cell, and Caco-2 cell
-
His6-tagged enzyme is expressed in Escherichia coli Rosetta (DE3) cells
-
expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
-, Q58579
; structural gene FAD1, essential yeast protein, disruption of the gene induces a lethal phenotype, cloned from a genomic library, vector pATH26 transformed into Saccharomyces cerevisiae and Escherichia coli RR1 on a multicopy plasmid
P38913, -
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R297A
-, Q6FNA9
involved in substrate binding
E268A
-, Q59263
active, involved in riboflavin kinase activity
E268A
-
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme
E268D
-, Q59263
active, involved in riboflavin kinase activity
E268D
-
the mutant shows about wild type catalytic efficiencies for ATP and FMN
H28A
-, Q59263
loss of both riboflavin kinase and FAD synthetase activities
H28D
-, Q59263
loss of both riboflavin kinase and FAD synthetase activities
N210A
-, Q59263
active, involved in riboflavin kinase activity
N210A
-
the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme
N210D
-, Q59263
active, involved in riboflavin kinase activity
N210D
-
the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme
R161A
-, Q59263
active, residue R161 does not play a critical role in catalysis
R161D
-, Q59263
active, residue R161 does not play a critical role in catalysis
S164A
-, Q59263
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
S164D
-, Q59263
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T165A
-, Q59263
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T165D
-, Q59263
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T208A
-, Q59263
active, involved in riboflavin kinase activity
T208A
-
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme
T208D
-, Q59263
active, involved in riboflavin kinase activity
T208D
-
the mutant shows increased catalytic efficiency for FMN and increased catalytic efficiency for ATP compared to the wild type enzyme
C126S
-, Q58579
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity about 2times higher than that of the wild type enzyme. The activity of the mutant in presence of Co2+ is very low
additional information
Q0WS47, Q9FMW8
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity; recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
H31D
-, Q59263
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
additional information
-
C-terminal domain delta(1-182)
C143S
-, Q58579
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity approximately wild type activity. The activity of the mutant in presence of Co2+ is very low
additional information
-
functional expression does not confer roseoflavin resistance to a FAD-synthetase defective Bacillus subtilis strain
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
industrial production of FAD and FMN as nutrient additives, pharmaceuticals and biochemical agents
nutrition
-, Q59263
-
nutrition
Corynebacterium ammoniagenes ATCC6872
-
-
-