Literature summary for 2.6.1.112 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.

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Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Bacillus subtilis subsp. subtilis	D8V0F7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(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	-	?
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	?	-	?

Synonyms

Synonyms	Comment	Organism
aminotransferase V	-	Bacillus subtilis subsp. subtilis
PucG	-	Bacillus subtilis subsp. subtilis

Cofactor

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

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)