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Information on EC 3.6.1.18 - FAD diphosphatase
for references in articles please use BRENDA:EC3.6.1.18
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.18 FAD diphosphatase
IUBMB Comments
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 expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.6.1.18
-
3.6.1.9
-
3.1.4.1
- pyrophosphatases
-
ppi-generating
- nppase
showSynonyms
nucleotide pyrophosphatase, fad pyrophosphatase, tp0796, mg2+-dependent fad pyrophosphatase, metal-dependent fad pyrophosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-nucleotidase
-
-
-
-
FAD pyrophosphatase
FADS1
flavin adenine dinucleotide pyrophosphatase
-
-
-
-
flavine adenine dinucleotide pyrophosphatase
-
-
-
-
Ftp_Tp-like
metal-dependent FAD pyrophosphatase
Mg2+-dependent FAD pyrophosphatase
nucleotide phosphodiesterase
-
-
-
-
nucleotide pyrophosphatase
-
-
-
-
riboflavin adenine dinucleotide pyrophosphatase
-
-
-
-
riboflavine adenine dinucleotide pyrophosphatase
-
-
-
-
TP0796
additional information
FAD pyrophosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FAD + H2O = AMP + FMN
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
phosphorous acid anhydride hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37289-30-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-Man + H2O
Man-1-phosphate + GMP
-
Substrates: EC 3.6.1.9 activity
Products: -
Products: -
?
NDP + H2O
?
-
Substrates: cleaves A, G, C, U dinucleotides
Products: -
Products: -
?
NTP + H2O
?
-
Substrates: cleaves A, G, C, U trinucleotides
Products: -
Products: -
?
FAD + H2O
FMN + AMP
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FAD + H2O
FMN + AMP
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Hg2+
Mg2+
Mn2+
Na+
-
200 mM, about 80% of the FAD pyrophosphatase activity with K+
NH4+
-
200 mM, about 60% of the FAD pyrophosphatase activity with K+
Rb+
-
200 mM, about 70% of the FAD pyrophosphatase activity with K+
Zn2+
Mg2+
-
5 mM, about 50% of the FAD pyrophosphatase activity with Co2+
Mg2+
dependent on, metal-dependent enzyme, bimetal center in the crystal structure of Escherichia coli Ftp
Mn2+
-
5 mM, about 40% of the FAD pyrophosphatase activity with Co2+
Zn2+
-
5 mM, about 20% of the FAD pyrophosphatase activity with Co2+
Zn2+
-
reverses EDTA inhibition, inhibitory at concentrations above 0.1 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Ankylosis
Antagonistic interactions between osterix and pyrophosphate during cementum formation.
Cholestasis
Serum alkaline phosphatase, nucleotide pyrophosphatase, 5'-nucleotide and lipoprotein-X in cholestasis.
Cholestasis, Extrahepatic
Usefulness of serum nucleotide pyrophosphatase and phosphodiesterase I activities in classifying liver disease.
Confusion
Purification of a plant nucleotide pyrophosphatase as a protein that interferes with nitrate reductase and glutamine synthetase assays.
Diabetes Mellitus, Type 2
The association of ENPP1 K121Q with diabetes incidence is abolished by lifestyle modification in the diabetes prevention program.
Glioma
An ecto-nucleotide pyrophosphatase is one of the main enzymes involved in the extracellular metabolism of ATP in rat C6 glioma.
Hypophosphatasia
Concerted regulation of inorganic pyrophosphate and osteopontin by akp2, enpp1, and ank: an integrated model of the pathogenesis of mineralization disorders.
Hypophosphatasia
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.
Liver Diseases
Nucleotide pyrophosphatase and phosphodiesterase I. Demonstration of activity in normal serum, and an increase in cholestatic liver disease.
Liver Diseases
Usefulness of serum nucleotide pyrophosphatase and phosphodiesterase I activities in classifying liver disease.
Lymphoma
[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]
Neoplasms
Plasma membrane associated enzymes of mammary tumours as the biochemical indicators of metastasizing capacity. Analyses of enriched plasma membrane preparations.
Neoplasms
Specific requirements for Vgamma9Vdelta2 T cell stimulation by a natural adenylated phosphoantigen.
Neoplasms
[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]
Ossification of Posterior Longitudinal Ligament
The extent of ossification of posterior longitudinal ligament of the spine associated with nucleotide pyrophosphatase gene and leptin receptor gene polymorphisms.
Osteoarthritis
Decreased levels of nucleotide pyrophosphatase phosphodiesterase 1 are associated with cartilage calcification in osteoarthritis and trigger osteoarthritic changes in mice.
Plasmacytoma
Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1.
Spondylitis, Ankylosing
Decrease in serum nucleotide pyrophosphatase activity in ankylosing spondylitis.
Syphilis
Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
N-ethylmaleimide
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00003
-
at pH 7.5 in chloroplasts, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.0000384
-
at pH 8.5 in chloroplasts, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.000343
-
at pH 7.5 in mitochondria, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.000482
-
at pH 8.5 in mitochondria, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.6 - 5.6
-
55% of maximum activity at pH 3.6, 20% of maximum activity at pH 5.6
7 - 10
7 - 10
-
less than 10% of maximum activity at pH 7, 90% of maximum activity at pH 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional FAD diphosphatase/FAD:protein FMN transferase, activity of EC 2.7.1.180
UniProt
brenda
bifunctional FAD diphosphatase/FAD:protein FMN transferase, activity of EC 2.7.1.180
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
physiological function
additional information
evolution
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
evolution
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
evolution
FAD synthetase FADS1, encoded by the gene At5g03430, exists as an apparent fusion with an ancestral FAD pyrophosphatase, a feature conserved across plants. FADS1 does not show pyrophosphatase activity
evolution
-
FAD synthetase exists FADS1 as an apparent fusion with an ancestral FAD pyrophosphatase. Bifunctional FADS1 is capable of catalyzing both the formation and degradation of the FAD cofactor
evolution
-
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
-
physiological function
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
physiological function
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein
physiological function
-
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
-
additional information
the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
additional information
-
the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
additional information
the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
additional information
-
the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). APBE_TREPA
Treponema pallidum (strain Nichols)
362
1
39064
Swiss-Prot
Secretory Pathway (Reliability: 4)
Q0WQL6_ARATH
408
0
45413
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E169K
site-directed mutagenesis of the probabale catalytic site residue, the Ftp_EcE169K protein variant does not show binding of FAD, inactive mutant
Y60A
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
Y60N
site-directed mutagenesis, a single amino acid substitution converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like)
D284A
mutation eliminates the enzyme's dual activities, thereby underscoring the role of Mg2+ in the enzyme-catalyzed reactions
E244A
critical catalytic residue, may activate a water molecule for nucleophilic attack
H256A
critical catalytic residue, may neutralize the charge on the leaving group during attack
N55Y
complete loss of FAD hydrolyase activity, mutation converts the enzyme from an Mg2+-dependent FAD diphosphatase to an FAD-binding protein
R245A
critical catalytic residue, may neutralize the charge on the leaving group during attack
S240A
critical catalytic residue, may activate a water molecule for nucleophilic attack
T288A
mutation in metal binding residue, abolishes FAD diphosphatase activity
D284A
-
mutation eliminates the enzyme's dual activities, thereby underscoring the role of Mg2+ in the enzyme-catalyzed reactions
-
N55Y
-
complete loss of FAD hydrolyase activity, mutation converts the enzyme from an Mg2+-dependent FAD diphosphatase to an FAD-binding protein
-
S240A
-
critical catalytic residue, may activate a water molecule for nucleophilic attack
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 12 h, concentration below 0.2 mg/ml, 60% loss of activity, can be restored by adding ADP
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, R.S.F.; Ford, H.C.
Purification and characterization of 5'-nucleotidase/FAD pyrophosphatase from human placenta
Methods Enzymol.
280
424-436
1997
Homo sapiens
brenda
Ragab, M.H.; Brightwell, R.; Tappel, A.L.
Hydrolysis of flavin-adenine dinucleotide by rat liver lysosomes
Arch. Biochem. Biophys.
123
179-185
1968
Rattus norvegicus
brenda
Ravindranath, S.D.; Rao, N.A.
Studies on nucleotidases in plants: Part II - Isolation and properties of an enzyme hydrolyzing FAD at alkaline pH from mung bean seedlings (Phaseolus radiatus)
Indian J. Biochem.
5
137-142
1968
Vigna radiata var. radiata
-
brenda
Ravindranath, S.D.; Rao, N.A.
Nucleotidases in plants. III. Effect of metabolites on the enzyme hydrolyzing flavine adenine dinucleotide (FAD) from Phaseolus radiatus
Arch. Biochem. Biophys.
133
54-59
1969
Vigna radiata var. radiata
brenda
Mistuda, H.; Tsuge, H.; Tomozawa, Y.; Kawai, F.
On the enzymatic hydrolysis of FAD in spinach leaves
J. Vitaminol. (Kyoto)
16
31-38
1970
Spinacia oleracea
brenda
Ravindranath, S.D.; Rao, N.A.
Nucleotidases in plants: V. Purification and properties of an enzyme hydrolysing flavin adenine dinucleotide at acid pH value from Phaseolus radiatus
Indian J. Biochem. Biophys.
8
219-226
1971
Vigna radiata var. radiata
brenda
Akiyama, T.; Selhub, J.; Rosenberg, J.H.
FMN phosphatase and FAD pyrophosphatase in rat intestinal brush borders: Role in intestinal absorption of dietary riboflavin
J. Nutr.
112
263-268
1982
Rattus norvegicus
brenda
Byrd, J.C.; Fearney, F.J.; Kim, Y.S.
Rat intestinal nucleotide-sugar pyrophosphatase. Localization, partial purification, and substrate specificity
J. Biol. Chem.
260
7474-7480
1985
Rattus norvegicus
brenda
Okumura, M.
Purification and properties of the enzyme for hydrolysis of flavin adenine dinucleotide from blood plasma of rabbit
Nagoya Igaku
105
117-123
1983
Oryctolagus cuniculus
-
brenda
Kim, J.K.; Ezaki, J.; Himeno, M.; Kato, K.
Purification and characterization of flavine-adenine dinucleotide phosphohydrolase from rat liver lysosomal membranes
J. Biochem.
114
126-131
1993
Rattus norvegicus
brenda
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
Eur. J. Biochem.
249
777-785
1997
Rattus norvegicus
brenda
Sandoval, F.J.; Zhang, Y.; Roje, S.
Flavin nucleotide metabolism in plants: monofunctional enzymes synthesize FAD in plastids
J. Biol. Chem.
283
30890-30900
2008
Lathyrus oleraceus
brenda
Pallotta, M.L.
Evidence for the presence of a FAD pyrophosphatase and a FMN phosphohydrolase in yeast mitochondria: a possible role in flavin homeostasis
Yeast
28
693-705
2011
Saccharomyces cerevisiae
brenda
Deka, R.K.; Brautigam, C.A.; Liu, W.Z.; Tomchick, D.R.; Norgard, M.V.
The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis
J. Biol. Chem.
288
11106-11121
2013
Treponema pallidum (O83774), Treponema pallidum, Treponema pallidum Nichols (O83774)
brenda
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
mBio
6
e00519
2015
Treponema pallidum (O83774), Treponema pallidum, Treponema pallidum Nichols (O83774)
brenda
Deka, R.K.; Brautigam, C.A.; Liu, W.Z.; Tomchick, D.R.; Norgard, M.V.
Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm
MicrobiologyOpen
5
21-38
2016
Escherichia coli (P0AB85), Escherichia coli, Treponema pallidum (O83774), Treponema pallidum
brenda
Lynch, J.H.; Roje, S.
A higher plant FAD synthetase is fused to an inactivated FAD pyrophosphatase
J. Biol. Chem.
298
102626
2022
Arabidopsis thaliana (Q0WQL6), Chlamydomonas reinhardtii
brenda
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