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

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.6.1.15
-
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RECOMMENDED NAME
GeneOntology No.
FAD-AMP lyase (cyclizing)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FAD = AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
208349-48-8
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
FAD
AMP + riboflavin cyclic-4',5'-phosphate
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
enzyme-activating cation
additional information
-
Mg2+ , Ca2+, Zn2+, Ni2+, Cu2+, Fe3+, Li+, Na+, K+ not required for activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
activates
Mn2+
-
activates
additional information
-
thirty-five compounds structurally related to FAD tested
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 0.09
FAD
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.82 - 24.1
FAD
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000025
ADP
-
-
0.00005
ATP
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01 - 0.02
FMN cyclase activity, lysate supernatant of BL21 cells, pH7.5, 37°C
13
-
p-nitrophenyl-d-TMP as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
Co2+ as activating cation
8.5
-
Mn2+ as activating cation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59000
-
SDS-PAGE
59400
x * 59400, SDS-PAGE
100000
-
ultrafiltration
140000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59400, SDS-PAGE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mg/ml bovine serum albumin
-
-80°C, TE: buffer 20 mM Tris-HCl and 0.5 mM EDTA, pH 8.2 at 4°C, 10 months
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chromatography on DEAE-cellulose
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
-
expression in BL21 cells
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LINKS TO OTHER DATABASES (specific for EC-Number 4.6.1.15)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)