Information on EC 4.6.1.15 - FAD-AMP lyase (cyclizing)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Euarchontoglires

EC NUMBER
COMMENTARY
4.6.1.15
-
RECOMMENDED NAME
GeneOntology No.
FAD-AMP lyase (cyclizing)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FAD = AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
FAD AMP-lyase (riboflavin-cyclic-4',5'-phosphate-forming)
Requires Mn2+ or Co2+. While FAD was the best substrate tested [2], the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dAK
-
gene name
Flavine-adenine-dinucleotide cyclase
-
-
-
-
FMN cyclase
-
-
-
-
FMN cyclase
-
-
FMN cyclase/dha kinase
Q3LXA3
bifunctional enzyme
FMN cyclase/dha kinase
-
bifunctional enzyme
Rivoflavin cyclic phosphate synthase
-
-
-
-
TKFC
-
-
triokinase/FMN cyclase
-
-
CAS REGISTRY NUMBER
COMMENTARY
208349-48-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
female Wistar rats
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
-
?
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
?
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
?
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
-
?
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
Q3LXA3
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
-
?
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
?
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
enzyme-activating cation
Mn2+
-
enzyme-activating cation
Mn2+
-
dependent on
additional information
-
Mg2+ , Ca2+, Zn2+, Ni2+, Cu2+, Fe3+, Li+, Na+, K+ not required for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
Q3LXA3
inhibits the FMN cyclase activity
ATP
-
inhibits the FMN cyclase activity
ATP
-
competitive inhibitor
FAD
-
concentration higher than 0.1 mM
FAD
-
concentration higher than 0.3 mM
additional information
-
twelve nucleotidic compounds tested, not inhibited by FMN, cFMN, dADP, dATP, AMP
-
additional information
-
not inhibited by glycerol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
activates
Mn2+
-
activates
additional information
-
thirty-five compounds structurally related to FAD tested
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006 - 0.008
FAD
-
-
0.009
FAD
-
Mn2+, pH: 7.5
0.036 - 0.045
FAD
-
Mn2+, pH: 8.3
0.09
FAD
-
Co2+, pH: 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.82
FAD
-
Mn2+, pH: 7.5
19.3 - 24.1
FAD
-
Mn2+, pH: 8.3
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000025
ADP
-
-
0.00005
ATP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01 - 0.02
Q3LXA3
FMN cyclase activity, lysate supernatant of BL21 cells, pH7.5, 37C
13
-
p-nitrophenyl-d-TMP as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
-
Co2+ as activating cation
8.5
-
Mn2+ as activating cation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
59000
-
SDS-PAGE
441636
100000
-
ultrafiltration
441636
140000
-
gel filtration
441635, 441636
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q3LXA3
x * 59400, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 mg/ml bovine serum albumin
-
-80C, TE: buffer 20 mM Tris-HCl and 0.5 mM EDTA, pH 8.2 at 4C, 10 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q3LXA3
chromatography on DEAE-cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
-
expression in BL21 cells
Q3LXA3