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Literature summary extracted from

  • Ramazzina, I.; Costa, R.; Cendron, L.; Berni, R.; Peracchi, A.; Zanotti, G.; Percudani, R.
    An aminotransferase branch point connects purine catabolism to amino acid recycling (2010), Nat. Chem. Biol., 6, 801-806.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.112 expression in Escherichia coli Bacillus subtilis subsp. subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.112 to 2.05 A resolution. The crystal shows a dimer. The pyridoxal 5'-phosphate cofactor binds at the dimer interface, forming a Schiff base with residue K200 Bacillus subtilis subsp. subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.112 Bacillus subtilis subsp. subtilis D8V0F7
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.112 (S)-ureidoglycine + glyoxylate the amino donor substrate is the S enantiomer of ureidoglycine. Glyoxylate is the preferred acceptor Bacillus subtilis subsp. subtilis N-carbamoyl-2-oxoglycine + glycine
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 ?
2.6.1.112 additional information in the absence of an amino group acceptor, part of the ureidoglycine donates its amino group to the enzyme in a half-transamination reaction, and part of the ureidoglycine undergoes decay, producing the substrate necessary to complete the reaction. The enzyme is able to use various keto acids. No substrates: Ala, Asp, Glu, Ser, Val Bacillus subtilis subsp. subtilis ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.112 aminotransferase V
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 Bacillus subtilis subsp. subtilis
2.6.1.112 PucG
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 Bacillus subtilis subsp. subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.112 pyridoxal 5'-phosphate
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 Bacillus subtilis subsp. subtilis

General Information

EC Number General Information Comment Organism
2.6.1.112 physiological function PucG catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. This activity enables soil and gut bacteria to use the animal purine waste as a source of carbon and nitrogen. The same substrate provides both the amino group donor and, via its spontaneous decay, the amino group acceptor Bacillus subtilis subsp. subtilis