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Literature summary extracted from

  • Azuma, Y.; Zschoche, R.; Hilvert, D.
    The C-terminal peptide of Aquifex aeolicus riboflavin synthase directs encapsulation of native and foreign guests by a cage-forming lumazine synthase (2017), J. Biol. Chem., 292, 10321-10327 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.9 wild-type enzyme and the four deletion constructs are individually co-expressed with His6-tagged lumazine synthase in Escherichia coli. Lumazine synthase forms cage complexes with the cognate riboflavin synthase from Aquifex aeolicus when both proteins are co-produced in the cytosol of Escherichia coli. A 12-amino acid-long peptide at the C terminus of riboflavin synthase serves as a specific localization sequence responsible for targeting the guest to the protein compartment Aquifex aeolicus
2.5.1.78 lumazine synthase forms cage complexes with the cognate riboflavin synthase from Aquifex aeolicus when both proteins are co-produced in the cytosol of Escherichia coli. A 12-amino acid-long peptide at the C terminus of riboflavin synthase serves as a specific localization sequence responsible for targeting the guest to the protein compartment Aquifex aeolicus

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.9 DELTA1-180 variant that lacks the C-terminal extension the coiled-coil and C-terminal peptide (AaRS1-180) Aquifex aeolicus
2.5.1.9 DELTA1-196 variant that lacks the C-terminal extension (1-196). Substantial decrease in association efficiency with lumazine synthase is observed for the truncated variant Aquifex aeolicus
2.5.1.9 DELTA180-196 variant that lacks the C-terminal extension the coiled-coil segment (DELTA180-196). The mutant enzyme associated with lumazine synthase to an about 3fold higher extent than the full-length riboflavin synthase Aquifex aeolicus
2.5.1.9 W207A the mutant enzyme is taken up by lumazine synthase only 30% less efficiently than wild-type enzyme Aquifex aeolicus
2.5.1.78 additional information a 12-amino acid-long peptide at the C terminus of riboflavin synthase serves as a specific localization sequence responsible for targeting the guest to the protein compartment. Covalent fusion of this peptide tag to heterologous guest molecules leads to their internalization into lumazine synthase assemblies both in vivo and in vitro Aquifex aeolicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.9 2 6,7-dimethyl-8-(1-D-ribityl)lumazine Aquifex aeolicus
-
 riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
-
 ?
2.5.1.78 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil Aquifex aeolicus
-
 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.9 Aquifex aeolicus
-
-
-
2.5.1.78 Aquifex aeolicus
-
-
-
2.5.1.78 Aquifex aeolicus O66529
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.9 2 6,7-dimethyl-8-(1-D-ribityl)lumazine
-
 Aquifex aeolicus riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
-
 ?
2.5.1.78 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
-
 Aquifex aeolicus 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.9 homotrimer each subunit comprising two beta-barrel catalytic domains (residues 1-179), a coiled-coil segment (residues 180-195), and a structurally disordered C-terminal extension (residues 196-207) Aquifex aeolicus

Synonyms

EC Number Synonyms Comment Organism
2.5.1.78 lumazine synthase
-
 Aquifex aeolicus

General Information

EC Number General Information Comment Organism
2.5.1.9 metabolism lumazine synthase forms specific inclusion complexes with riboflavin synthase when both proteins are co-expressed in a heterologous host. Encapsulation of specific enzymes in self-assembling protein cages is a hallmark of bacterial compartments that function as counterparts to eukaryotic organelles Aquifex aeolicus
2.5.1.78 metabolism lumazine synthase forms specific inclusion complexes with riboflavin synthase when both proteins are co-expressed in a heterologous host. Encapsulation of specific enzymes in self-assembling protein cages is a hallmark of bacterial compartments that function as counterparts to eukaryotic organelles Aquifex aeolicus
2.5.1.78 physiological function lumazine synthase forms cage complexes with the cognate riboflavin synthase when both proteins are coproduced in the cytosol of Escherichia coli. A 12-amino acid-long peptide at the C terminus of riboflavin synthase serves as a specific localization sequence responsible for targeting the guest to the protein compartment Aquifex aeolicus