3.6.1.18: FAD diphosphatase
This is an abbreviated version!
For detailed information about FAD diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.18
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3.6.1.18
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3.6.1.9
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3.1.4.1
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pyrophosphatases
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ppi-generating
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nppase
- 3.6.1.18
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3.6.1.9
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3.1.4.1
- pyrophosphatases
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ppi-generating
- nppase
Reaction
Synonyms
5'-nucleotidase, FAD diphosphatase, FAD pyrophosphatase, FADppase, flavin adenine dinucleotide pyrophosphatase, flavine adenine dinucleotide pyrophosphatase, Ftp_Ec, Ftp_Tp-like, metal-dependent FAD pyrophosphatase, Mg2+-dependent FAD pyrophosphatase, More, nucleotide phosphodiesterase, nucleotide pyrophosphatase, riboflavin adenine dinucleotide pyrophosphatase, riboflavine adenine dinucleotide pyrophosphatase, TP0796
ECTree
3.6.1.18 FAD diphosphataseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.1.18 - FAD diphosphatase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like) (EC 3.6.1.18). The engineered protein variant (Ftp_EcY60A) shows Mg2+-dependent FAD diphosphatase activity, but also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate, indicating that the protein variant enzyme has dual activity. The Ftp_EcY60A protein variant binds FAD, yet rapidly hydrolyzes it and the product FMN dissociates
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additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like) (EC 3.6.1.18). The engineered protein variant (Ftp_EcY60A) shows Mg2+-dependent FAD diphosphatase activity, but also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate, indicating that the protein variant enzyme has dual activity. The Ftp_EcY60A protein variant binds FAD, yet rapidly hydrolyzes it and the product FMN dissociates
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additional information
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in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate
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additional information
?
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in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate
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?
additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. It also displays FAD diphosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (EC 3.6.1.18)
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additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. It also displays FAD diphosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (EC 3.6.1.18)
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additional information
?
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in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate
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?
additional information
?
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-
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. It also displays FAD diphosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (EC 3.6.1.18)
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