Literature summary for 2.5.1.9 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 .

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

Protein Variants

Protein Variants	Comment	Organism
DELTA1-180	variant that lacks the C-terminal extension the coiled-coil and C-terminal peptide (AaRS1-180)	Aquifex aeolicus
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
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
W207A	the mutant enzyme is taken up by lumazine synthase only 30% less efficiently than wild-type enzyme	Aquifex aeolicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 6,7-dimethyl-8-(1-D-ribityl)lumazine	Aquifex aeolicus	-	riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine	-	?

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 6,7-dimethyl-8-(1-D-ribityl)lumazine	-	Aquifex aeolicus	riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine	-	?

Subunits

Subunits	Comment	Organism
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

General Information

General Information	Comment	Organism
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