Literature summary for 3.4.21.105 extracted from

Foo, A.C.; Harvey, B.G.; Metz, J.J.; Goto, N.K.
Influence of hydrophobic mismatch on the catalytic activity of Escherichia coli GlpG rhomboid protease (2015), Protein Sci., 24, 464-473.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
purification of the catalytic transmembrane domain of GlpG into phosphocholine or maltoside detergent micelles of varying alkyl chain lengths. Catalytic turnover numbers depend on detergent alkyl chain length, with saturated chains containing 10-12 carbon atoms supporting maximal activity. Similar results are obtained in phospholipid bicelles, with no proteolytic activity being detected in longer-chain lipids. Hydrophobic mismatch gives rise to a small change in structure and can exert an inhibitory effect on rhomboid activity	Escherichia coli

Purification (Comment)

Organism

purification of the catalytic transmembrane domain of GlpG into phosphocholine or maltoside detergent micelles of varying alkyl chain lengths. Catalytic turnover numbers depend on detergent alkyl chain length, with saturated chains containing 10-12 carbon atoms supporting maximal activity. Similar results are obtained in phospholipid bicelles, with no proteolytic activity being detected in longer-chain lipids. Hydrophobic mismatch gives rise to a small change in structure and can exert an inhibitory effect on rhomboid activity

Escherichia coli

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Release 2023.1 (January 2023)