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

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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 ACCESSION NO.
LITERATURE
FAD = AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Flavine-adenine-dinucleotide cyclase
-
-
-
-
FMN cyclase
-
-
-
-
FMN cyclase/dha kinase
Q3LXA3
bifunctional enzyme
FMN cyclase/dha kinase
-
bifunctional enzyme
Rivoflavin cyclic phosphate synthase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
208349-48-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
female Wistar rats
-
-
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
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 ACCESSION NO.
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
enzyme-activating cation
Mn2+
-
enzyme-activating cation
additional information
-
Mg2+ , Ca2+, Zn2+, Ni2+, Cu2+, Fe3+, Li+, Na+, K+ not required for activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-, Q3LXA3
inhibits the FMN cyclase activity
ATP
-
inhibits the FMN cyclase activity
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Co2+
-
activates
Mn2+
-
activates
additional information
-
thirty-five compounds structurally related to FAD tested
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.82
-
FAD
-
Mn2+, pH: 7.5
19.3
24.1
FAD
-
Mn2+, pH: 8.3
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.5e-05
-
ADP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.3
-
-
Co2+ as activating cation
8.5
-
-
Mn2+ as activating cation
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
59000
-
-
SDS-PAGE
100000
-
-
ultrafiltration
140000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q3LXA3
x * 59400, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
-
-, Q3LXA3
chromatography on DEAE-cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in BL21 cells
-, Q3LXA3