The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.
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SYSTEMATIC NAME
IUBMB Comments
FAD nucleotidohydrolase
The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.
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
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
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)
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)
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)
Concerted regulation of inorganic pyrophosphate and osteopontin by akp2, enpp1, and ank: an integrated model of the pathogenesis of mineralization disorders.
Sustained osteomalacia of long bones despite major improvement in other hypophosphatasia-related mineral deficits in tissue nonspecific alkaline phosphatase/nucleotide pyrophosphatase phosphodiesterase 1 double-deficient mice.
[Demonstration of nucleotide pyrophosphatase and phosphohydrolase activities in normal lymphocyte of Balb/c mice and absence of these activities in YC8 tumor cells and in lymphocytes of animals with YC8 lymphoma]
Plasma membrane associated enzymes of mammary tumours as the biochemical indicators of metastasizing capacity. Analyses of enriched plasma membrane preparations.
[Demonstration of nucleotide pyrophosphatase and phosphohydrolase activities in normal lymphocyte of Balb/c mice and absence of these activities in YC8 tumor cells and in lymphocytes of animals with YC8 lymphoma]
The extent of ossification of posterior longitudinal ligament of the spine associated with nucleotide pyrophosphatase gene and leptin receptor gene polymorphisms.
Decreased levels of nucleotide pyrophosphatase phosphodiesterase 1 are associated with cartilage calcification in osteoarthritis and trigger osteoarthritic changes in mice.
Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.
a single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like). 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 flavin-trafficking protein (Ftp) in the syphillis spirochete Treponema pallidum (Ftp_Tp) is a bacterial metal-dependent FAD diphosphatase that hydrolyzes FAD into AMP and FMN in the periplasm
the flavin-trafficking protein (Ftp) in the syphillis spirochete Treponema pallidum (Ftp_Tp) is a bacterial metal-dependent FAD diphosphatase that hydrolyzes FAD into AMP and FMN in the periplasm
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified Ftp_Ec mutant variant Y60N complexed with ADP, hanging drop vapor diffusion method, mixing of 0.004 ml of 20 mg/ml protein in Tris, pH 7.5, and 20 mM NaCl, with 0.04 ml of reservoir solution containing 0.2 M NH4NO3, and 20% w/v PEG 3350, and 0.001 ml of 50 mM MgCl2, and 0.001 ml of 50 mM ADP, 20°C, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement and modelling
apo-enzyme and in complex with FAD, AMP and Mn2+, Mg2+, to 1.45-2.3 A resolution. The enzyme adopts the canonical ApbE superfamily fold and has a unique bimetal Mg2+ catalytic center. Isoform TP0796 is a monomer in the crystalline lattice
site-directed mutagenesis, 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
site-directed mutagenesis, a single amino acid substitution converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like)
Studies on nucleotidases in plants: Part II - Isolation and properties of an enzyme hydrolyzing FAD at alkaline pH from mung bean seedlings (Phaseolus radiatus)
Barile, M.; Brizio, C.; de Virgilio, C.; Delfine, S.; Quagliariello, E.; Passarella, S.
Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver: The occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
Deka, R.; Brautigam, C.; Liu, W.; Tomchick, D.; Norgard, M.
Evidence for posttranslational protein flavinylation in the syphilis spirochete treponema pallidum: Structural and biochemical insights from the catalytic core of a periplasmic flavin-trafficking protein
Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm