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Literature summary for 3.4.21.105 extracted from

  • Baker, R.P.; Young, K.; Feng, L.; Shi, Y.; Urban, S.
    Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate (2007), Proc. Natl. Acad. Sci. USA, 104, 8257-8262.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.105

Protein Variants

Protein Variants Comment Organism
D243A site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Escherichia coli
F133Y/F135Y site-directed mutagenesis, almost inactive mutant Escherichia coli
F139S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
F153A/W236A site-directed mutagenesis, the enzyme shows 10fold increased activity compared to the wild-type enzyme Escherichia coli
F245A site-directed mutagenesis, the enzyme shows increased activity compared to the wild-type enzyme Escherichia coli
G199A site-directed mutagenesis, inactive mutant Escherichia coli
G257A site-directed mutagenesis, inactive mutant Escherichia coli
H145A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
H254A site-directed mutagenesis, inactive mutant Escherichia coli
L143S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
L229V/F232V/W236V site-directed mutagenesis, the enzyme shows 4fold increased activity compared to the wild-type enzyme Escherichia coli
L244A site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Escherichia coli
M247A site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Escherichia coli
M249A site-directed mutagenesis, the enzyme shows increased activity compared to the wild-type enzyme Escherichia coli
additional information engineered mutants in the L1 loop and active-site region of the GlpG rhomboid protease suggest an important structural, rather than dynamic, gating function for the L1 loop, conversely, three classes of mutations that promote transmembrane helix 5 displacement away from the protease core dramatically enhance enzyme activity 4 to 10fold Escherichia coli
N154A site-directed mutagenesis, almost inactive mutant Escherichia coli
N251A site-directed mutagenesis, inactive mutant Escherichia coli
R137A site-directed mutagenesis, inactive mutant Escherichia coli
S201A site-directed mutagenesis, inactive mutant Escherichia coli
W136A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
W157A/F232A site-directed mutagenesis, the enzyme shows 6fold increased activity compared to the wild-type enzyme Escherichia coli
W157C/F232C site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme Escherichia coli
Y138D site-directed mutagenesis, inactive mutant Escherichia coli
Y138F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y138S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y138S/F139S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y138S/F139S/L143S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y138Y site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y160C/L229C site-directed mutagenesis, the enzyme shows highly reduced activity compared to the wild-type enzyme Escherichia coli
Y205A site-directed mutagenesis, inactive mutant Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information local perturbations around the active site hinder proteolytic activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane intramembrane enzyme, contains a ring of transmembrane segments Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli intramembrane proteolysis is a core regulatory mechanism of cells that raises a biochemical paradox of how hydrolysis of peptide bonds is accomplished within the normally hydrophobic environment of the membrane ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P09391
-
-

Reaction

Reaction Comment Organism Reaction ID
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains transmembrane helix 5 is the lateral substrate gate, the enzyme contains a catalytic serine recessed into the plane of the membrane, within a hydrophilic cavity that opens to the extracellular face, but protected laterally from membrane lipids by a ring of transmembrane segments, structure-function analysis, transmembrane helix 5 movement to gate lateral substrate entry is a rate-limiting step in intramembrane proteolysis Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information intramembrane proteolysis is a core regulatory mechanism of cells that raises a biochemical paradox of how hydrolysis of peptide bonds is accomplished within the normally hydrophobic environment of the membrane Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
rhomboid intramembrane protease
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 Escherichia coli