Literature summary for 1.5.5.2 extracted from

Srivastava, D.; Zhu, W.; Johnson, W.H.; Whitman, C.P.; Becker, D.F.; Tanner, J.J.
The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction (2010), Biochemistry, 49, 560-569.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
2.15 A resolution structure of the PRODH inactivated by N-propargylglycine. The initial events involved in broadcasting the reduced flavin state to the distal membrane-binding domain include major reorganization of the flavin ribityl chain, severe butterfly bending of the isoalloxazine ring, and disruption of an electrostatic network involving the flavin N(5) atom, Arg431, and Asp370. The active site is incompletely assembled in the absence of the substrate, and the binding of proline draws together conserved residues in helix 8 and the beta1-alphal loop to complete the active site	Escherichia coli

Crystallization (Comment)

Organism

2.15 A resolution structure of the PRODH inactivated by N-propargylglycine. The initial events involved in broadcasting the reduced flavin state to the distal membrane-binding domain include major reorganization of the flavin ribityl chain, severe butterfly bending of the isoalloxazine ring, and disruption of an electrostatic network involving the flavin N(5) atom, Arg431, and Asp370. The active site is incompletely assembled in the absence of the substrate, and the binding of proline draws together conserved residues in helix 8 and the beta1-alphal loop to complete the active site

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
N-propargylglycine	irreversibly inactivates PutA by covalently linking the flavin N(5) atom to the epsilon-amino of Lys329. Inactivation locks PutA into a conformation that may mimic the proline-reduced, membrane-associated form	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09546	-	-

Synonyms

Synonyms	Comment	Organism
PutA	-	Escherichia coli

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Release 2023.1 (January 2023)