Literature summary for 3.4.21.105 extracted from

Xue, Y.; Ha, Y.
The catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate (2012), J. Biol. Chem., 287, 3099-3107.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitors 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate, to 2.3 A resolution. Enzyme forms a covalent adduct with diisopropyl fluorophosphonate, which mimics the oxyanion-containing tetrahedral intermediate of the hydrolytic reaction. The oxyanion is stabilized by the main chain amide of residue Ser201 and by the side chains of His150 and Asn154. The phosphorylation of the catalytic Ser201 weakens its interaction with His254, causing the catalytic histidine to rotate away from the serine and accompanied by further rearrangement of the side chains of Tyr205 and Trp236 within the substrate-binding groove and by opening of the L5 cap and movement of transmembrane helix S5 toward S6 in a direction different from that predicted by the lateral gating model	Escherichia coli
rhomboid protease GlpG in complex with 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate, sitting drop vapor diffusion method, using 100 mM Bis-Tris propane (pH 7.0), and 3 M NaCl	Escherichia coli

Crystallization (Comment)

Organism

in complex with inhibitors 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate, to 2.3 A resolution. Enzyme forms a covalent adduct with diisopropyl fluorophosphonate, which mimics the oxyanion-containing tetrahedral intermediate of the hydrolytic reaction. The oxyanion is stabilized by the main chain amide of residue Ser201 and by the side chains of His150 and Asn154. The phosphorylation of the catalytic Ser201 weakens its interaction with His254, causing the catalytic histidine to rotate away from the serine and accompanied by further rearrangement of the side chains of Tyr205 and Trp236 within the substrate-binding groove and by opening of the L5 cap and movement of transmembrane helix S5 toward S6 in a direction different from that predicted by the lateral gating model

Escherichia coli

rhomboid protease GlpG in complex with 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate, sitting drop vapor diffusion method, using 100 mM Bis-Tris propane (pH 7.0), and 3 M NaCl

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
3,4-dichloroisocoumarin	mechanism-based inhibitor	Escherichia coli
diisopropyl fluorophosphonate	irreversible inhibition; mechansim-based inhibitor	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli	P09391	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3,4-dichloroisocoumarin + H2O	a significant portion of the inhibitor 3,4-dichloroisocoumarin bound to GlpG is enzymatically turned over	Escherichia coli	?	-	?
BODIPY FL casein + H2O	-	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
GlpG	-	Escherichia coli
rhomboid protease	-	Escherichia coli