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Information on EC 3.4.24.78 - gpr endopeptidase and Organism(s) Priestia megaterium and UniProt Accession P22321

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.78 gpr endopeptidase
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This record set is specific for:
Priestia megaterium
UNIPROT: P22321 not found.
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Word Map
  • 3.4.24.78
  • cohesin
  • anaphase
  • chromatid
  • securin
  • spindle
  • aneuploidy
  • centromeres
  • metaphase-to-anaphase
  • rad21
  • disjunction
  • kinetochore
  • centriole
  • kleisin
  • separase-dependent
  • missegregation
  • sister-chromatides
  • degradation
  • synthesis
The taxonomic range for the selected organisms is: Priestia megaterium
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala
Synonyms
germinating-specific protease, GPS, germination proteinase, GPR, tepA, YmfB, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
germinating-specific protease, GPS
-
-
-
-
germination proteinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
75718-32-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GPR zymogen + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Phe-Glu-Ile-Ala-Ser-Glu-Phe-Gly-Val-Asn-Leu-Gly-Pro-Asp-Ala-Thr-Ala-Arg + H2O
N-acetyl-Phe-Glu + Ile-Ala-Ser-Glu-Phe-Gly-Val-Asn-Leu-Gly-Pro-Asp-Ala-Thr-Ala-Arg
show the reaction diagram
-
-
-
?
N-acetyl-Thr-Glu-Phe-Ala + H2O
N-acetyl-Thr-Glu + Phe-Ala
show the reaction diagram
-
-
-
?
N-acetyl-Thr-Glu-Phe-Ala-Ser-Glu-Phe + H2O
N-acetyl-Thr-Glu + Phe-Ala-Ser-Glu-Phe
show the reaction diagram
-
-
-
?
purified small acid-soluble protein + H2O
?
show the reaction diagram
-
-
-
-
?
small acid-soluble protein + H2O
?
show the reaction diagram
-
-
-
-
?
small tetra-to heptapeptides containing a cleavage site + H2O
?
show the reaction diagram
-
-
-
-
?
spore protein A + H2O
fragments of spore protein A
show the reaction diagram
-
specific sequence of cleavage site, R-Glu-(Phe,Ile)-Ala,Gly-Ser-Glu-R, gpr endopeptidase cleaves at the first glutamyl bond
-
?
spore protein B + H2O
fragments of spore protein B
show the reaction diagram
-
specific sequence of cleavage site, R-Glu-(Phe,Ile)-Ala,Gly-Ser-Glu-R, gpr endopeptidase cleaves at the first glutamyl bond
-
?
spore protein C + H2O
fragments of spore protein C
show the reaction diagram
-
specific sequence of cleavage site, R-Glu-(Phe,Ile)-Ala,Gly-Ser-Glu-R, gpr endopeptidase cleaves at the first glutamyl bond
-
?
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
small acid-soluble protein + H2O
?
show the reaction diagram
-
-
-
-
?
spore protein A + H2O
fragments of spore protein A
show the reaction diagram
-
specific sequence of cleavage site, R-Glu-(Phe,Ile)-Ala,Gly-Ser-Glu-R, gpr endopeptidase cleaves at the first glutamyl bond
-
-
?
spore protein B + H2O
fragments of spore protein B
show the reaction diagram
-
specific sequence of cleavage site, R-Glu-(Phe,Ile)-Ala,Gly-Ser-Glu-R, gpr endopeptidase cleaves at the first glutamyl bond
-
-
?
spore protein C + H2O
fragments of spore protein C
show the reaction diagram
-
specific sequence of cleavage site, R-Glu-(Phe,Ile)-Ala,Gly-Ser-Glu-R, gpr endopeptidase cleaves at the first glutamyl bond
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
gpr is likely to be regulated by metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not inhibited by EDTA, 1,10-phenanthroline, DFP, N-ethylmaleimide, iodoacetamide or by inhibitors of aspartic proteases
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
N-acetyl-Phe-Glu-Ile-Ala-Ser-Glu-Phe-Gly-Val-Asn-Leu-Gly-Pro-Asp-Ala-Thr-Ala-Arg
-
pH 7.4, 37°C
20
N-acetyl-Thr-Glu-Phe-Ala-Ser-Glu-Phe
-
pH 7.4, 37°C
0.014
purified small acid-soluble protein
-
-
-
20
small tetra-to heptapeptides containing a cleavage site
-
-
-
0.0014
spore protein A
-
spore protein A, Km lower than 0.014 mM
-
0.008
spore protein B
-
Km lower than 0.008 mM
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
4 * 40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
4 * 40000
tetramer
-
wild-type P46 nearly 100% tetrameric, P41 largely tetrameric but also with a significant percentage of lower-molecular-mass-species
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 3 A resolution
-
truncated enzyme termed P30, hanging-drop vapor-diffusion, mixing 0.002 ml of protein and 0.002 ml of reservoir solution containing 32% polyethylene glycol 4000, 100 mM Tris-HCl, pH 8.3 at room temperature, crystals of P30 appear within 4 d, crystals diffract to about 3.3 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D127A
-
no activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
D127E
-
no activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
D127N
-
no activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
D127S
-
no activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
D153N
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
D193N
-
no activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
D211N
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
D246N
-
partial activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
D253N
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
D256N
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
E201Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
E26Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
E89Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
H125Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
H142Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
K21P
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
K223A
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
K223E
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
K223H
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
K223M
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
Q208E
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
R202Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
R224Q
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
S199A
-
activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
S210A
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
S212A
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
S218A
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
S249A
-
partial activity of P41 against small acid-soluble spore protein, no autoprocessing of P46
T125N
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
T173V
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
T215V
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
T74D
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
Y72F
-
activity of P41 against small acid-soluble spore protein, autoprocessing of P46
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
subcloned into the pET23a vector, overexpression of full-length gene P46 and a truncated form encoding only P41 in Escherichia coli Bl21(DE3)pLysS
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
-
D127 and D193 are essential for activity and autoprocessing
synthesis
-
the enzyme is synthesized only during sporulation within the developing spore, and as a zymogen, ca. 2 h after its synthesis the zymogen autoprocesses to the active enzyme by intramolecular removal of 15 N-terminal residues
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dignam, S.S.; Setlow, P.
Bacillus megaterium spore protease. Action of the enzyme on peptides containing the amino acid sequence cleaved by the enzyme in vivo
J. Biol. Chem.
255
8408-8412
1980
Priestia megaterium, Priestia megaterium QN 8155
Manually annotated by BRENDA team
Ponnuraj, K.; Kelly, S.; Nessi, C.; Setlow, P.; Jedrzejas, M.J.
Crystallization and preliminary diffraction studies of a truncated form of a novel protease from spores of Bacillus megaterium
Acta Crystallogr. Sect. D
56
70-72
2000
Priestia megaterium
Manually annotated by BRENDA team
Pei, J.; Grishin, N.V.
Breaking the singleton of germination protease
Protein Sci.
11
691-697
2002
Priestia megaterium (P22321)
Manually annotated by BRENDA team
Setlow, P.
Endopeptidase GPR
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
983-984
2004
Bacillus anthracis, Bacillus cereus, Bacillus subtilis, Halalkalibacterium halodurans, Oceanobacillus iheyensis, Priestia megaterium
-
Manually annotated by BRENDA team
Carroll, T.M.; Setlow, P.
Site-directed mutagenesis and structural studies suggest that the germination protease, GPR, in spores of Bacillus species is an atypical aspartic acid protease
J. Bacteriol.
187
7119-7125
2005
Priestia megaterium
Manually annotated by BRENDA team