Information on EC 3.4.21.105 - rhomboid protease

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.4.21.105
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RECOMMENDED NAME
GeneOntology No.
rhomboid protease
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
713145-02-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
no activity in Encephalitozoon cuniculi
nearly ubiquitous enzyme family
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Manually annotated by BRENDA team
no activity in Methanothermobacter thermoautotrophicus
nearly ubiquitous enzyme family
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Manually annotated by BRENDA team
no activity in Thermoplasma volcanium
nearly ubiquitous enzyme family
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Manually annotated by BRENDA team
no activity in Xylella fastidiosa
nearly ubiquitous enzyme family
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain XD37
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
TgROM1
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Manually annotated by BRENDA team
TgROM2
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Manually annotated by BRENDA team
TgROM3
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Manually annotated by BRENDA team
TgROM4
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Manually annotated by BRENDA team
TgROM5
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dichloroisocoumarin + H2O
?
show the reaction diagram
-
a significant portion of the inhibitor 3,4-dichloroisocoumarin bound to GlpG is enzymatically turned over
-
-
?
adhesin + H2O
?
show the reaction diagram
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EhROM1 is able to cleave Plasmodium adhesins but not the canonical substrate Drosophila Spitz. It is examined whether EhROM1 can cleave a representative of each of the four families of Plasmodium adhesins: the EBL adhesin BAEBL, the RBL adhesin Rh4, AMA1, and TRAP. All adhesins are efficient substrates for the recoded EhROM1 with the exception of AMA1, which is cleaved less well than the others by EhROM1
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-
?
adhesin BAEBL + H2O
?
show the reaction diagram
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substrate of ROM1 and ROM4
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-
?
adhesin CTRP + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin EBA-175 + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin EBP-175 + H2O
?
show the reaction diagram
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adhesin EBP-175 of Plasmodium falciparum undergoes ectodomain shedding, in a reaction catalyzed by plasmodium rhomboid pfROM4. pfROM4 cleaves within the transmembrane region of the adhesin
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-
?
adhesin JESEBL + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
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-
?
adhesin MAEBL + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
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-
?
adhesin MIC2 + H2O
?
show the reaction diagram
adhesin MTRAP + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin PFF0800c + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh1 + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh24 + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2a + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
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-
?
adhesin Rh2b + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin TRAP + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesion protein from Toxoplasma gondii + H2O
?
show the reaction diagram
alpha chain of pre-T cell receptor + H2O
?
show the reaction diagram
constitutively active receptor variant required for T cell development. cleavage contributes to ER-associated degradation, cleavage productsare translocated and degraded by the proteasome
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-
?
apical membrane antigen 1 + H2O
?
show the reaction diagram
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i.e. AMA1, substrate only of ROM1
-
-
?
apical membrane antigen AMA1 + H2O
?
show the reaction diagram
-
-
-
?
APP-Spi7-Flag + H2O
?
show the reaction diagram
-
-
-
-
?
beta-lactamase Spitz transmembrane domain + H2O
?
show the reaction diagram
-
34 residue peptide, sequence KRPRPMLEKASIASGAMCALVFMLFVCLAFYLRK
-
-
?
beta-lactamase-Spitz transmembrane segment-maltose binding protein + H2O
?
show the reaction diagram
-
a fusion protein containing the Spitz TM segment fused to globular proteins at the N- and C-termini (beta-lactamase and maltose binding protein, respectively)
-
-
?
Bla-GknTM-MBP + H2O
?
show the reaction diagram
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recombinantly expressed fusion protein having the transmembrane region of Gurken, GknTM, a physiological substrate of Drosophila rhomboids, GlpG cleaves an extramembrane region of the substrate exposed to the periplasm, overview
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?
BODIPY FL casein + H2O
?
show the reaction diagram
C100Spi-Flag + H2O
?
show the reaction diagram
C100Tat-Flag + H2O
?
show the reaction diagram
C100Tat-Flag is a chimera of the C-terminal 100 residues of APP, with seven residues of the Pseudomonas stuartii TatA cleavage site substituted at the N-terminus
-
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?
Ccp1 + H2O
?
show the reaction diagram
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Ccp1 is a mitochondrial cytochrome c peroxidase its cleavage side resides in a short stretch of moderately hydrophobic sequence
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?
chaperone Star + H2O
?
show the reaction diagram
chimeric protein of the bacterial pelB leader peptide, GFP as the extracellularectodomain, the juxtamembrane-transmembrane-cytosolic residues 122-230 of Spitz and a C-terminal epitope + H2O
?
show the reaction diagram
CyPet-TatA-YPet + H2O
?
show the reaction diagram
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engineered substrate based on transmembrane substrate TatA from Providencia stuartii, suitable for FRET assay
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?
cytochrome c peroxidase + H2O
processed cytochrome c peroxidase + targeting sequence peptide
show the reaction diagram
-
cleaving the targeting sequence of cytochrome c peroxidase, Pcp1
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?
cytochrome c peroxidase Ccp1 + H2O
?
show the reaction diagram
-
cleavage of Ccp1 by Pcp1/Rbd1 appears to occur directly after or within its hydrophobic sorting sequence
-
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?
cytochrome c peroxidase precursor + H2O
cytochrome c peroxidase + ?
show the reaction diagram
Delta-transmembrane domain + H2O
?
show the reaction diagram
dynamin-like GTPase + H2O
?
show the reaction diagram
-
-
-
-
?
ephrin B3 + H2O
?
show the reaction diagram
epidermal growth factor + H2O
?
show the reaction diagram
-
efficient and specific substrate for rhomboid protease RHBDL2
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-
?
FL-casein + H2O
?
show the reaction diagram
growth factor Spitz + H2O
?
show the reaction diagram
growth-factor gurken + H2O
?
show the reaction diagram
-
-
-
-
?
growth-factor spitz + H2O
?
show the reaction diagram
-
-
-
-
?
Gurken + H2O
?
show the reaction diagram
Gurken protein + H2O
?
show the reaction diagram
-
-
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?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
show the reaction diagram
Gurken-derived peptide + H2O
?
show the reaction diagram
Gurken-transmembrane domain + H2O
?
show the reaction diagram
Keren + H2O
?
show the reaction diagram
Keren protein + H2O
?
show the reaction diagram
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-
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
show the reaction diagram
LacY trans-membrane domain 2 + H2O
?
show the reaction diagram
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
show the reaction diagram
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
show the reaction diagram
lectin + H2O
?
show the reaction diagram
-
EhROM1 is able to cleave cell surface lectin
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?
Mgm1 + H2O
?
show the reaction diagram
Mgm1p + H2O
?
show the reaction diagram
MIC adhesin + H2O
?
show the reaction diagram
microneme protein MIC2 + H2O
?
show the reaction diagram
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-
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?
microneme protein MIC6 + H2O
?
show the reaction diagram
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-
-
?
myelin protein zero mutant L170R + H2O
?
show the reaction diagram
mutant form is unstable and efficiently cleaved by isoform RHBDL4. Wild-type myelin protein zero is not a substrate
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?
N-acetyl-PEG4-QRKVRMAHIVFSFPC-amide + H2O
N-acetyl-PEG4-QRKVRMA + HIVFSFPC-amide
show the reaction diagram
olycystin-1 + H2O
?
show the reaction diagram
11-TM spanning membrane protein. Isoform RHBDL4 cleaves several truncated versions of polycystin-1 at luminal loops or juxtamembrane transmembrane regions. Wild-type olycystin-1 is not a substrate
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?
Opa-1 + H2O
?
show the reaction diagram
-
genetic analysis shows that Opa1 and Parl are part of the same pathway, with Parl positioned upstream of Opa1 in the control of apoptosis
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?
opsin mutant bearing TCRalpha degron motif + H2O
?
show the reaction diagram
opsin-degron mutant is degraded by isoform RHBDL4, whereas the wild-type protein is stable
-
-
?
phosphoglycerate mutase 5 + H2O
?
show the reaction diagram
mitochondrial Ser/Thr protein phosphatase PGAM5
substrate is cleaved in its N-terminal transmembrane domain in response to mitochondrial membrane potential loss and mediated by presenilin-associated rhomboid-like protein. In response to membrane potential loss, the enzyme dissociates from substrate PINK1, a mitochondrial Ser/Thr protein kinase, and reciprocally associates with substrate PGAM5. Results suggest that the enzyme mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria
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?
Protein + H2O
?
show the reaction diagram
-
cleaves a model protein having an N-terminal and periplasmically localized beta-lactamase domain, a LacY-derived transmembrane region, and a cytosolic maltose binding protein mature domain, cleavage occurs between Ser and Asp in a region of high local hydrophilicity, which might be located iin a juxtamembrane rather than an intramembrane position. The conserved Ser and His residue of GlpG are esential for proteolytic activity
-
-
?
protein Bla-LY2-MBP + H2O
?
show the reaction diagram
protein Gurken + H2O
?
show the reaction diagram
protein Keren + H2O
?
show the reaction diagram
protein MIC2 + H2O
?
show the reaction diagram
-
cleavage at an Ala-Gly bond
-
-
?
protein Spitz + H2O
?
show the reaction diagram
reporter substrate LY2
?
show the reaction diagram
-
using a combinatorial approach it is shown that a negatively charged residue is the primary determinant of cleavage. The amino acid preceding peptide bond hydrolysis (the P1 position) has a preference for the small and polar Ser residue. The amino acid succeeding peptide bond hydrolysis (the P1 position) has a preference for negatively charged Asp
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-
?
Spitz + H2O
?
show the reaction diagram
Spitz protein + H2O
?
show the reaction diagram
Spitz-polyA + H2O
?
show the reaction diagram
-
-
-
-
?
Spitz-transmembrane domain + H2O
?
show the reaction diagram
TatA + H2O
?
show the reaction diagram
TatA + H2O
processed TatA + N-terminal extension peptide
show the reaction diagram
TatA protein + H2O
?
show the reaction diagram
-
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
show the reaction diagram
thrombomodulin + H2O
?
show the reaction diagram
thrombomodulin + H2O
soluble thrombomodulin + ?
show the reaction diagram
-
-
-
-
?
Tic40 + H2O
?
show the reaction diagram
-
i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
trans-membrane domain + H2O
?
show the reaction diagram
trans-membrane domain Gurken + H2O
?
show the reaction diagram
TRAP protein + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adhesin BAEBL + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin CTRP + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin EBA-175 + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin JESEBL + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin MAEBL + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin MIC2 + H2O
?
show the reaction diagram
Q695T8
-
-
-
?
adhesin MTRAP + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin PFF0800c + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh1 + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh24 + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2a + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin Rh2b + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
adhesin TRAP + H2O
?
show the reaction diagram
-
substrate of ROM1 and ROM4
-
-
?
apical membrane antigen 1 + H2O
?
show the reaction diagram
-
i.e. AMA1, substrate only of ROM1
-
-
?
chaperone Star + H2O
?
show the reaction diagram
-
cleavage of Star within its transmembrane domain both in cell culture and in flies, the enzyme is involved in regulation of levels of Spitz, the major Drosophila EGF receptor ligand, mechanism for modulating the activity of Star, thereby influencing the levels of active Spitz ligand, intracellular trafficking of Spitz isimpaired by Rhomboid-dependent cleavage of Star, overview
-
-
?
cytochrome c peroxidase + H2O
processed cytochrome c peroxidase + targeting sequence peptide
show the reaction diagram
-
cleaving the targeting sequence of cytochrome c peroxidase, Pcp1
-
-
?
ephrin B3 + H2O
?
show the reaction diagram
-
RHBDL-2 mediated proteolytic processing may regulate intercellular interactions between ephrinB3 and eph receptors
-
-
?
epidermal growth factor + H2O
?
show the reaction diagram
-
efficient and specific substrate for rhomboid protease RHBDL2
-
-
?
growth factor Spitz + H2O
?
show the reaction diagram
growth-factor gurken + H2O
?
show the reaction diagram
-
-
-
-
?
growth-factor spitz + H2O
?
show the reaction diagram
-
-
-
-
?
Gurken + H2O
?
show the reaction diagram
-
-
-
-
?
Gurken protein + H2O
?
show the reaction diagram
-
-
-
-
?
Gurken protein + H2O
PQRKVRMA + HIVFSFFV
show the reaction diagram
Gurken-derived peptide + H2O
?
show the reaction diagram
Keren + H2O
?
show the reaction diagram
-
-
-
-
?
Keren protein + H2O
?
show the reaction diagram
-
-
-
-
?
l-Mgm1 + H2O
s-Mgm1 + N-terminal putative transmembrane segment
show the reaction diagram
-
rhomboid-type protease Pcp1 is essential for wild type mitochondrial morphology. The processing of the large isoform l-Mgm1 by rhomboid-type protease Pcp1 to s-Mgm1, and the presence of both isoforms of Mgm1 appears to be crucial for wild-type mitochondrial morphology and maintenance of mitochondrial DNA
-
-
?
LacYTM2 protein + H2O
DINHISKS + DTGIIFAA
show the reaction diagram
large isoform of Mgm1 + H2O
short isoform of Mgm1 + ?
show the reaction diagram
-
the enzyme is involved in the pathway of Mgm1 biogenesis. A strong shift in the ratio between both isoform of Mgm1 is sufficient to alter mitochondrial morphology
-
-
?
lectin + H2O
?
show the reaction diagram
-
EhROM1 is able to cleave cell surface lectin
-
-
?
Mgm1 + H2O
?
show the reaction diagram
-
cleaving the long isoform of Mgm1 to produce the short one
-
-
?
MIC adhesin + H2O
?
show the reaction diagram
protein Gurken + H2O
?
show the reaction diagram
-
-
-
-
?
protein Keren + H2O
?
show the reaction diagram
-
-
-
-
?
protein Spitz + H2O
?
show the reaction diagram
Spitz + H2O
?
show the reaction diagram
Spitz protein + H2O
?
show the reaction diagram
TatA + H2O
processed TatA + N-terminal extension peptide
show the reaction diagram
TatA protein + H2O
?
show the reaction diagram
-
-
-
-
?
TatA protein + H2O
MESTIATA + AFGSPWQL
show the reaction diagram
thrombomodulin + H2O
soluble thrombomodulin + ?
show the reaction diagram
-
-
-
-
?
Tic40 + H2O
?
show the reaction diagram
-
i.e. the chloroplast inner envelope translocon component of 40 kDa
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S,4S)-1-[(4-chlorophenyl)sulfonyl]-3-methyl-4-phenylazetidin-2-one
(3S,4S)-3-methyl-1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
1,2-dihexanoyl-sn-glycero-3-phosphocholine
-
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity
1,2-dimyristoyl-sn-glycero-3-phosphocholine
-
paGlpG purified in detergent causes 5% reduction in activity
1-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
1-(biphenyl-3-ylsulfonyl)-4-phenylazetidin-2-one
1-(biphenyl-4-ylsulfonyl)-4-phenylazetidin-2-one
1-myristoyl-sn-glycero-3-phosphocholine
-
paGlpG purified in detergent causes 10% reduction in activity
1-palmitoyl-sn-glycero-3-phospho-rac-(1-glycerol)
-
paGlpG purified in detergent causes 20% reduction in activity
1-[(3'-methylbiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
1-[(3-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
1-[(3-chlorophenyl)sulfonyl]-4-(2-phenylethyl)azetidin-2-one
1-[(3-chlorophenyl)sulfonyl]-4-(propan-2-yl)azetidin-2-one
1-[(4'-chlorobiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
1-[(4-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
1-[(4-chlorophenyl)sulfonyl]-3-methylazetidin-2-one
1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
2-methylpropyl 2-oxo-4-phenylazetidine-1-carboxylate
-
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site
3,3,3-trifluoro-N-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-2-(trifluoromethyl)propanamide
3,3,3-trifluoro-N-[2-(propan-2-yloxy)phenyl]-2-(trifluoromethyl)propanamide
3,4-dichloroisocoumarin
3-methyl-1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
-
-
3-[(3-cholamidopropyl)-dimethylammonio]-1-propansulfonate
-
1,2-dimyristoyl-sn-glycero-3-phosphocholine additionally added, paGlpG purified in detergent causes 37% reduction in activity
4-(2-chlorophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
4-(3-bromophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
4-[(3-methyl-2-oxoazetidin-1-yl)sulfonyl]benzonitrile
7-amino-3-butoxy-4-chloro-1H-isochromen-1-one
-
-
7-amino-4-chloro-3-(2-phenylethoxy)-1H-isochromen-1-one
-
-
7-amino-4-chloro-3-methoxyisocoumarin
-
-
7-amino-4-chloro-3-[(5-phenylpentyl)oxy]-1H-isochromen-1-one
-
-
acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone
-
inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner
acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone
-
inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
cyclopentyl 2-oxo-4-phenylazetidine-1-carboxylate
-
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site
dichloroisocoumarin
diisopropyl fluorophosphonate
-
irreversible inhibition; mechansim-based inhibitor
dodecyl maltoside
-
paGlpG purified in detergent causes 77% reduction in activity
N-(2,6-dimethylphenyl)-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
n-nonyl-beta-D-glucoside
-
paGlpG purified in detergent causes 45% reduction in activity
N-[2-(cyclopentyloxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
N-[2-(cyclopropylmethoxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
tert-butyl 2-[[3,3,3-trifluoro-2-(trifluoromethyl)propanoyl]amino]benzoate
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
plastid translocon component Tic40
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00074 - 0.0029
BODIPY FL casein
-
0.0039
CyPet-TatA-YPet
-
K0.5 value, Hill coefficient 1.8, pH 6.0, 3°C
-
0.0018 - 0.0065
FL-casein
-
0.0076 - 0.119
TatA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.0073
BODIPY FL casein
-
0.0028
CyPet-TatA-YPet
Providencia stuartii
-
pH 6.0, 3°C
-
0.06 - 0.063
FL-casein
-
0.0017 - 0.07
TatA
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 7.78
BODIPY FL casein
161016
0.7
CyPet-TatA-YPet
Providencia stuartii
-
pH 6.0, 3°C
202294
2.48 - 33
FL-casein
202295
0.08 - 2.37
TatA
67632
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
(3S,4S)-1-[(4-chlorophenyl)sulfonyl]-3-methyl-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.03
(3S,4S)-3-methyl-1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0038
1-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.014
1-(biphenyl-3-ylsulfonyl)-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.041
1-(biphenyl-4-ylsulfonyl)-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.043
1-[(3'-methylbiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.016
1-[(3-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.033
1-[(3-chlorophenyl)sulfonyl]-4-(2-phenylethyl)azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.085
1-[(3-chlorophenyl)sulfonyl]-4-(propan-2-yl)azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.047
1-[(4'-chlorobiphenyl-4-yl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.026
1-[(4-bromophenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.026
1-[(4-chlorophenyl)sulfonyl]-3-methylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.074
1-[(4-methylphenyl)sulfonyl]-4-phenylazetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0033
3,3,3-trifluoro-N-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0023
3,3,3-trifluoro-N-[2-(propan-2-yloxy)phenyl]-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0183
4-(2-chlorophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0068
4-(3-bromophenyl)-1-[(3-chlorophenyl)sulfonyl]azetidin-2-one
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.02
4-[(3-methyl-2-oxoazetidin-1-yl)sulfonyl]benzonitrile
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0004
7-amino-3-butoxy-4-chloro-1H-isochromen-1-one
Escherichia coli
-
pH 7.3, 37°C
0.0011
7-amino-4-chloro-3-(2-phenylethoxy)-1H-isochromen-1-one
Escherichia coli
-
pH 7.3, 37°C
0.006
7-amino-4-chloro-3-methoxyisocoumarin
Escherichia coli
-
in 50 mM HEPES-NaOH (pH 7.5), 0.4 M NaCl, 5 mM EDTA, 10% (v/v) glycerol, and 0.05% (w/v) n-dodecyl-beta-D-maltoside, at 37°C
0.00075
7-amino-4-chloro-3-[(5-phenylpentyl)oxy]-1H-isochromen-1-one
Escherichia coli
-
pH 7.3, 37°C
0.029
benzyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidine-2-carboxylate
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.017
N-(2,6-dimethylphenyl)-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0018
N-[2-(cyclopentyloxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.001
N-[2-(cyclopropylmethoxy)phenyl]-3,3,3-trifluoro-2-(trifluoromethyl)propanamide
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.182
phenyl 2-oxo-4-phenylazetidine-1-carboxylate
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
0.0013
tert-butyl 2-[[3,3,3-trifluoro-2-(trifluoromethyl)propanoyl]amino]benzoate
Providencia stuartii
-
25 mM HEPES, pH 7.4, 5 mM EDTA, 5% (v/v) glycerol, 0.5% (w/v) DDM, 20% (v/v) DMSO, at 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
-
more active at 25°C than at 37°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
-
much more active az 37°C than at 25°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
Rhomboid-3
Manually annotated by BRENDA team
ROM1 is localized to a single, thread-like structure on one side of the merozoites that appears to be in close proximity to the subpellicular microtubules, ROM1 is not associated with micronemes, rhoptries, or dense granules, the three identified secretory organelles of invasion, immunohistochemic detection, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in blood stage merozoites, PbROM1 localizes to the apical end where proteins involved in invasion are also present
Manually annotated by BRENDA team
-
membrane-embedded, traverses the membrane six times
-
Manually annotated by BRENDA team
-
membranes of the late endosome compartment
Manually annotated by BRENDA team
-
intramembrane enzyme
Manually annotated by BRENDA team
-
EhROM1 is an active intramembrane serine protease
-
Manually annotated by BRENDA team
merozoite apical pole and the posterior pole, a single thread-like organelle in merozoites, immunohistochemic detection, overview
Manually annotated by BRENDA team
additional information