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Information on EC 4.6.1.15 - FAD-AMP lyase (cyclizing) and Organism(s) Rattus norvegicus

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IUBMB Comments
Requires Mn2+ or Co2+. While FAD was the best substrate tested , 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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Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fmn cyclase, fad-amp lyase (cyclizing), triokinase/fmn cyclase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Flavine-adenine-dinucleotide cyclase
-
-
-
-
FMN cyclase
-
-
-
-
FMN cyclase/dha kinase
-
bifunctional enzyme
Rivoflavin cyclic phosphate synthase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
208349-48-8
-
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
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
enzyme-activating cation
Mn2+
-
enzyme-activating cation
additional information
-
Mg2+ , Ca2+, Zn2+, Ni2+, Cu2+, Fe3+, Li+, Na+, K+ not required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
twelve nucleotidic compounds tested, not inhibited by FMN, cFMN, dADP, dATP, AMP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
activates
Mn2+
-
activates
additional information
-
thirty-five compounds structurally related to FAD tested
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 0.09
FAD
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.82 - 24.1
FAD
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000025
ADP
-
-
0.00005
ATP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13
-
p-nitrophenyl-d-TMP as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
Co2+ as activating cation
8.5
-
Mn2+ as activating cation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TKFC_RAT
578
0
59444
Swiss-Prot
other Location (Reliability: 2)
A0A8I6AF41_RAT
527
0
54502
TrEMBL
other Location (Reliability: 2)
A0A8I6AR90_RAT
586
0
60549
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
ultrafiltration
140000
-
gel filtration
59000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fraiz, F.J.; Pinto, R.M.; Costas, M.J.; Avalos, M.; Canales, J.; Cabezas, A.; Cameselle, J.C.
Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver
Biochem. J.
330
881-888
1998
Rattus norvegicus
-
Manually annotated by BRENDA team
Cabezas, A.; Pinto, R.M.; Fraiz, F.; Canales, J.; Gonzalez-Santiago, S.; Cameselle, J.C.
Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): Preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion
Biochemistry
40
13710-13722
2001
Rattus norvegicus
Manually annotated by BRENDA team
Cabezas, A.; Costas, M.J.; Pinto, R.M.; Couto, A.; Cameselle, J.C.
Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases
Biochem. Biophys. Res. Commun.
338
1682-1689
2005
Homo sapiens (Q3LXA3), Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team