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Literature summary for 2.7.1.28 extracted from

  • Rodrigues, J.R.; Cameselle, J.C.; Cabezas, A.; Ribeiro, J.M.
    Closure of the human TKFC active site comparison of the apoenzyme and the complexes formed with either triokinase or FMN cyclase substrates (2019), Int. J. Mol. Sci., 20, 1099 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glyceraldehyde Homo sapiens
-
 ADP + D-glyceraldehyde 3-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q3LXA3 bifunctional triokinase/FMN cyclase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glyceraldehyde
-
 Homo sapiens ADP + D-glyceraldehyde 3-phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
hTKFC
-
 Homo sapiens
TKFC
-
 Homo sapiens

General Information

General Information Comment Organism
evolution hTKFC is functionally and structurally similar to Citrobacter sp. DHA kinase Homo sapiens
additional information study of the flexibility of dimeric hTKFC starting with its active sites in an open conformation, molecular dynamics simulation of the structural model of hTKFC containing the kinase substrates dihydroxyacetone (DHA covalently bound to His221) and ATP. Enzyme structure homology modelling using the crystal structure of Citrobacter sp. DHA kinase. The normal-mode analysis of hTKFC models confirms the trend of K domains to approach L domains, different modes, overview Homo sapiens
physiological function human triokinase/flavin mononucleotide (FMN) cyclase (hTKFC) is a bifunctional enzyme which catalyzes the adenosine triphosphate (ATP)-dependent phosphorylation of D-glyceraldehyde (GA) and dihydroxyacetone (DHA), and also the Mn2+-dependent splitting of flavin adenine dinucleotide (FAD) by an internal cyclizing reaction that forms adenosine monophosphate (AMP) and riboflavin 4',5'-phosphate or cyclic FMN Homo sapiens