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Literature summary for 3.6.1.18 extracted from

  • 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 (2015), mBio, 6, e00519.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.18

Cloned(Commentary)

Cloned (Comment) Organism
-
 Treponema pallidum

Protein Variants

Protein Variants Comment Organism
D284A mutation eliminates the enzyme's dual activities, thereby underscoring the role of Mg2+ in the enzyme-catalyzed reactions Treponema pallidum
E244A critical catalytic residue, may activate a water molecule for nucleophilic attack Treponema pallidum
H256A critical catalytic residue, may neutralize the charge on the leaving group during attack Treponema pallidum
K165A mutation enhances the FAD diphosphatase activity Treponema pallidum
K165E mutation enhances the FAD diphosphatase activity Treponema pallidum
N55Y complete loss of FAD hydrolyase activity, mutation converts the enzyme from an Mg2+-dependent FAD diphosphatase to an FAD-binding protein Treponema pallidum
R245A critical catalytic residue, may neutralize the charge on the leaving group during attack Treponema pallidum
S240A critical catalytic residue, may activate a water molecule for nucleophilic attack Treponema pallidum
T288A mutation in metal binding residue, abolishes FAD diphosphatase activity Treponema pallidum

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Treponema pallidum
-
-

Organism

Organism UniProt Comment Textmining
Treponema pallidum O83774 bifunctional FAD diphosphatase/FAD:protein FMN transferase, activity of EC 2.7.1.180
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Treponema pallidum Nichols O83774 bifunctional FAD diphosphatase/FAD:protein FMN transferase, activity of EC 2.7.1.180
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate Treponema pallidum ?
-
 ?
additional information in addition, enzyme flavinylates protein(s) covalently with FMN on a threonine side chain of an appropriate sequence motif using FAD as the substrate Treponema pallidum Nichols ?
-
 ?