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Information on EC 3.4.21.10 - acrosin and Organism(s) Ovis aries and UniProt Accession Q9GL10

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.10 acrosin
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Ovis aries
UNIPROT: Q9GL10 not found.
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Word Map
The taxonomic range for the selected organisms is: Ovis aries
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
preferential cleavage: Arg-/-, Lys-/-
Synonyms
acrosin, sperm acrosin, beta-acrosin, alpha-acrosin, acrosomal proteinase, acrosomal protease, acrosin amidase, acrosin ii, psi-acrosin, acrosin i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acrosin
trypsin-like serine protease of the S1 family
53 kDa fucose-binding protein
-
-
-
-
acrosin amidase
-
-
-
-
acrosomal protease
-
-
-
-
acrosomal proteinase
-
-
-
-
acrozonase
-
-
-
-
alpha-acrosin
-
-
-
-
beta-acrosin
-
-
-
-
proteinase, acrosomal
-
-
-
-
psi-acrosin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-57-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
proacrosin + H2O
acrosin + peptide
show the reaction diagram
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester hydrochloride + H2O
?
show the reaction diagram
-
-
-
-
?
toluene-p-sufonyl-L-arginine methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
toluene-p-sulfonyl-L-arginine methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
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
proacrosin + H2O
acrosin + peptide
show the reaction diagram
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(4'-aminophenoxypropoxy)benzamidine
-
-
Aprotinin
-
-
benzamidine
-
-
butan-1-ol
-
-
Ca2+
-
-
suramin
-
compound with combined antifertility agent and microbicide, three to four molecules of suramin bind to one molecule of enzyme
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
activated by 2-methylpropan-2-ol, dimethyl sulfoxide and some other water-miscible solvents
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
Nalpha-benzoyl-L-arginine ethyl ester hydrochloride
-
-
0.021
toluene-p-sulfonyl-L-arginine methyl ester
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49
methyl N2-[(4-methylphenyl)sulfonyl]-L-argininate
-
-
115 - 162
Nalpha-benzoyl-L-Arg ethyl ester
-
-
additional information
additional information
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACRO_SHEEP
329
0
36119
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36119
x * 36119, calculated from the deduced amino acid sequence
38000
-
x * 38000, SDS-PAGE, beta-acrosin
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 36119, calculated from the deduced amino acid sequence
?
-
x * 38000, SDS-PAGE, beta-acrosin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals grown in the presence of 10 mM 4-aminobenzamidine by vapor diffusion, complex of the enzyme with 4-aminobenzamidine, crystal structure solved to 2.1 and 2.9 A resolution
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes
-
freeze-drying: beta-acrosin: very stable
-
more, psi-acrosin: unstable
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brown, C.R.; Hartree, E.F.
Studies on ram acrosin. Activation of proacrosin accompanying the isolation of acrosin from spermatozoa, and purification of the enzyme by affinity chromatography
Biochem. J.
175
227-238
1978
Ovis aries
Manually annotated by BRENDA team
Brown, C.R.; Andani, Z.; Hartree, E.F.
Studies on ram acrosin. Isolation from spermatozoa, activation by cations and organic solvents, and influence of cations on its reaction with inhibitors
Biochem. J.
149
133-146
1975
Ovis aries
Manually annotated by BRENDA team
Hermans, J.M.; Haines, D.S.; James, P.S.; Jones, R.
Kinetics of inhibition of sperm beta-acrosin activity by suramin
FEBS Lett.
544
119-122
2003
Ovis aries, Sus scrofa
Manually annotated by BRENDA team
Tranter, R.; Read, J.A.; Jones, R.; Brady, R.L.
Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin
Structure Fold. Des.
8
1179-1188
2000
Sus scrofa (P08001), Ovis aries (Q9GL10)
Manually annotated by BRENDA team
Raterman, D.; Springer, M.S.
The molecular evolution of acrosin in placental mammals
Mol. Reprod. Dev.
75
1196-1207
2008
Amblysomus hottentotus (B0LM06), Bos taurus (P79343), Bradypus tridactylus (B0LM16), Canis lupus familiaris, Cavia porcellus (Q60491), Cynocephalus volans (B0LM30), Diceros bicornis (B0LM26), Dugong dugon (B0LM13), Echinops telfairi (B0LM07), Elephantulus edwardii (B0LM09), Equus caballus (B0LM27), Erethizon dorsatum (B0LM36), Euphractus sexcinctus (B0LM17), Felis catus (B0LM18), Galegeeska rufescens (B0LM10), Homo sapiens (P10323), Homo sapiens, Hystrix brachyura (B0LM35), Lama glama (B0LM21), Loxodonta africana (B0LM12), Macaca mulatta, Macroscelides proboscideus (B0LM11), Manis sp. DMR-2008 (B0LM29), Mus musculus (Q3ZB05), Ochotona princeps (B0LM32), Orycteropus afer (B0LM15), Oryctolagus cuniculus (P48038), Otospermophilus beecheyi (B0LM38), Ovis aries (Q9GL10), Pan troglodytes (B0LM34), Procavia capensis (B0LM08), Puma concolor (B0LM19), Rattus fuscipes (B0LM37), Rattus norvegicus (P29293), Sorex cinereus (B0LM24), Sus scrofa (P08001), Sylvilagus floridanus (B0LM33), Tadarida brasiliensis (B0LM23), Talpa europaea (B0LM25), Tapirus pinchaque (B0LM28), Tragelaphus angasii (B0LM22), Trichechus manatus (B0LM14), Tupaia glis (B0LM31), Tursiops truncatus (B0LM20)
Manually annotated by BRENDA team