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Information on EC 3.4.24.84 - Ste24 endopeptidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8RX88

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.84 Ste24 endopeptidase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8RX88 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
The peptide bond hydrolysed can be designated -C-/-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids
Synonyms
zmpste24, ste24p, face-1, atste24, afc1p, hs ste24p, a-factor converting enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ste24p
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
316364-97-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a-factor + H2O
fragments of a-factor
show the reaction diagram
-
-
?
CaM53 + H2O
fragments of CaM53
show the reaction diagram
CaM53 is a prenylated C2+-calmodulin from petunia
-
?
RACU88402 + H2O
fragments of RACU88402
show the reaction diagram
RACU88402 is a Rac-like GTPase
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
zinc metalloprotease motif HEXXH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 21% inhibition, inhibition is not reversible
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 76% inhibition, inhibition is not reversible
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
hydropathy blot analysis suggests 7 membrane-spanning domains
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FACE1_ARATH
424
4
48482
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48455
x * 48455, deduced from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 48455, deduced from nucleotide sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of AtSte24 in Sacchromyces cerevisiae ste24DELTA mutant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bracha, K.; Lavy, M.; Yalovsky, S.
The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
J. Biol. Chem.
277
29856-29864
2002
Homo sapiens (O75844), Saccharomyces cerevisiae (P47154), Saccharomyces cerevisiae, Arabidopsis thaliana (Q8RX88)
Manually annotated by BRENDA team
Porter, S.B.; Hildebrandt, E.R.; Breevoort, S.R.; Mokry, D.Z.; Dore, T.M.; Schmidt, W.K.
Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones
Biochim. Biophys. Acta
1773
853-862
2007
Arabidopsis thaliana, Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team