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Information on EC 3.4.21.105 - rhomboid protease and Organism(s) Haemophilus influenzae and UniProt Accession P44783

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.105 rhomboid protease
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This record set is specific for:
Haemophilus influenzae
UNIPROT: P44783 not found.
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Word Map
  • 3.4.21.105
  • flap
  • drosophila
  • medial
  • dorsal
  • posterior
  • ventral
  • glossitis
  • midline
  • trapezius
  • shoulder
  • thalamic
  • scapula
  • fossa
  • pilonidal
  • reuniens
  • serratus
  • paraventricular
  • levator
  • er-associated
  • intercostal
  • ventromedial
  • ventrolateral
  • mediodorsal
  • intralaminar
  • parafascicular
  • sacrococcygeal
  • abduct
  • electromyographic
  • paracentral
  • retrotranslocation
  • aesthetic
  • latissimus
  • cheilitis
  • birefringent
  • erector
  • anteroventral
  • nicastrin
  • anteromedial
  • supraspinatus
  • incerta
  • clavicle
  • myofascial
  • site-2
  • argos
  • extradural
  • seromas
  • petrous
  • infraspinatus
  • gurken
  • glenohumeral
  • analysis
  • medicine
  • molecular biology
The taxonomic range for the selected organisms is: Haemophilus influenzae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
Synonyms
rhomboid, derlin-1, rhbdd1, rhomboid protease, intramembrane protease, rhbdl2, rhbdl4, rhomboid protein, ehrom1, rho-4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
rhomboid structure and catalytic mechanism, catalytic dyad id formed by S201 and H254, structure-function modeling
CAS REGISTRY NUMBER
COMMENTARY hide
713145-02-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
?
FL-casein + H2O
?
show the reaction diagram
-
-
-
?
TatA + H2O
?
show the reaction diagram
transmembrane substrate from Providencia stuartii. Binding of TatA occurs with positive cooperativity in an exosite-mediated mode of substrate binding. Exosite formation is dependent on the oligomeric state of rhomboids, and when dimers are dissociated, allosteric substrate activation is not observed
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
regulation, overview
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065
FL-casein
pH 6.0, 3°C
-
0.119
TatA
K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.063
FL-casein
pH 6.0, 3°C
-
0.07
TatA
pH 6.0, 3°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.7
FL-casein
pH 6.0, 3°C
-
0.59
TatA
pH 6.0, 3°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
intramembrane enzyme with 6 transmembrane segments
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135100
protein with detergent bound, sedimentation equilibrium result
22124
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
61967
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F137A
the mutant shows 14% of the wild type activity
F144A
the mutation results in a 42% decrease in activity compared with the wild type enzyme
F160A
the mutant decreases peptidase activity by 54% compared to wild type enzyme
F68A
the substitution has no effect on activity (98% activity compared to the wild type enzyme)
F76A
the mutation results in a 95% decrease in activity compared with the wild type enzyme
F84A
the mutant shows 5% of the wild type activity
L136A
the mutant shows 22% of the wild type activity
M164A
the mutant decreases peptidase activity by 40% compared to wild type enzyme
W72A
the mutant is not expressed and activity cannot be assessed
W72A/F76A/F144A
the three alanine substitutions result in a 2.5fold increase in activity compared to wild type enzyme
W72V/F76V/F144V
the three valine substitutions result in a 2fold increase in activity compared to wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Top10 cells
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lemberg, M.K.; Freeman, M.
Cutting proteins within lipid bilayers: rhomboid structure and mechanism
Mol. Cell
28
930-940
2007
Drosophila melanogaster, Escherichia coli, Haemophilus influenzae (P44783)
Manually annotated by BRENDA team
Brooks, C.L.; Lazareno-Saez, C.; Lamoureux, J.S.; Mak, M.W.; Lemieux, M.J.
Insights into substrate gating in H. influenzae rhomboid
J. Mol. Biol.
407
687-697
2011
Haemophilus influenzae (P44783), Haemophilus influenzae
Manually annotated by BRENDA team
Sampathkumar, P.; Mak, M.W.; Fischer-Witholt, S.J.; Guigard, E.; Kay, C.M.; Lemieux, M.J.
Oligomeric state study of prokaryotic rhomboid proteases
Biochim. Biophys. Acta
1818
3090-3097
2012
Escherichia coli, Bacillus spizizenii (E0U436), Haemophilus influenzae (P44783), Haemophilus influenzae, Escherichia coli DH5alpha, Bacillus spizizenii ATCC 23059 (E0U436), Haemophilus influenzae ATCC 51907 (P44783)
Manually annotated by BRENDA team
Arutyunova, E.; Panwar, P.; Skiba, P.M.; Gale, N.; Mak, M.W.; Lemieux, M.J.
Allosteric regulation of rhomboid intramembrane proteolysis
EMBO J.
33
1869-1881
2014
Escherichia coli, Haemophilus influenzae (P44783), Haemophilus influenzae, Providencia stuartii (P46116), Haemophilus influenzae ATCC 51907 (P44783)
Manually annotated by BRENDA team