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Information on EC 4.6.1.15 - FAD-AMP lyase (cyclizing) and Organism(s) Homo sapiens and UniProt Accession Q3LXA3

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EC Tree
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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This record set is specific for:
Homo sapiens
UNIPROT: Q3LXA3
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
FMN cyclase/dha kinase
bifunctional enzyme
Flavine-adenine-dinucleotide cyclase
-
-
-
-
FMN cyclase
Rivoflavin cyclic phosphate synthase
-
-
-
-
TKFC
-
-
triokinase/FMN cyclase
-
-
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
-
-
-
?
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
Mn2+
-
dependent on
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
inhibits the FMN cyclase activity
ATP
-
competitive inhibitor
additional information
-
not inhibited by glycerol
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TKFC_HUMAN
575
0
58947
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59400
x * 59400, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59400, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in BL21 cells
expressed in Escherichia coli BL21 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Rodrigues, J.R.; Couto, A.; Cabezas, A.; Pinto, R.M.; Ribeiro, J.M.; Canales, J.; Costas, M.J.; Cameselle, J.C.
Bifunctional homodimeric triokinase/FMN cyclase: contribution of protein domains to the activities of the human enzyme and molecular dynamics simulation of domain movements
J. Biol. Chem.
289
10620-10636
2014
Homo sapiens
Manually annotated by BRENDA team