Information on EC 3.4.24.38 - gametolysin

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The expected taxonomic range for this enzyme is: Chlamydomonas reinhardtii

EC NUMBER
COMMENTARY
3.4.24.38
-
RECOMMENDED NAME
GeneOntology No.
gametolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-/-Arg-Phe-Ala
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cell wall lytic enzyme
-
-
Chlamydomonas cell wall degrading protease
-
-
-
-
Chlamydomonas reinhardtii metalloproteinase
-
-
-
-
Gamete autolysin
-
-
Gamete lytic enzyme
-
-
-
-
Gamete lytic enzyme
-
-
Gametolysin
-
-
-
-
GLE
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
97089-74-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
green alga, wild-type strain 137c
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-neoendorphin + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
poor substrate
-
-
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
polypeptides derived from casein
show the reaction diagram
-
not
-
-
-
casein + H2O
polypeptides derived from casein
show the reaction diagram
-
alpha- and beta-casein, poor substrate
-
-
Cell wall protein + H2O
?
show the reaction diagram
-
cell wall lytic enzyme, reaction involved in cell fusion during mating of Chlamydomonas reinhardtii gametes
-
-
-
Cell wall protein + H2O
?
show the reaction diagram
-
released during agglutination of gametes of opposite mating type
-
-
-
Chlamydomonas cell wall polypeptide + H2O
?
show the reaction diagram
-
2 polypeptides (peptide 2, MW 294000, and 5, MW 215000) of 16 polypeptides, i.e. the NaClO4-insoluble fraction, disintegrates cell wall structure by acting on only a few salt-insoluble components
-
-
-
dynorphin(1-13) + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Heat-denatured collagen + H2O
?
show the reaction diagram
-
-
-
-
-
Leu-Trp-Met-Arg-Phe-Ala + H2O
Leu-Trp-Met + Arg-Phe-Ala + Leu-Trp + Met-Arg-Phe-Ala
show the reaction diagram
-
-
-
-
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
Proteins rich in proline and hydroxyproline + H2O
?
show the reaction diagram
-
-
-
-
-
RNAse A + H2O
Lower MW polypetides
show the reaction diagram
-
-
-
-
Zoosporangia cell walls + H2O
?
show the reaction diagram
-
-
-
-
-
Zoosporangia cell walls + H2O
?
show the reaction diagram
-
glutaraldehyde-fixed
-
-
-
Zoosporangia cell walls + H2O
?
show the reaction diagram
-
selected domains within walls of gametes, zoospores or zoosporangia
-
-
-
Mastoparan + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
bovine serum albumin
-
-
-
additional information
?
-
-
insulin B-chain
-
-
-
additional information
?
-
-
hemoglobin, casein, poly(Pro) or poly(hydroxyproline), Chlamydomonas reinhardtii has a second cell wall lytic enzyme, a sporangial autolysin
-
-
-
additional information
?
-
-
no substrates are cytochrome c, lysozyme, myoglobin, trypsin inhibitor, ovalbumin
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Cell wall protein + H2O
?
show the reaction diagram
-
cell wall lytic enzyme, reaction involved in cell fusion during mating of Chlamydomonas reinhardtii gametes
-
-
-
Cell wall protein + H2O
?
show the reaction diagram
-
released during agglutination of gametes of opposite mating type
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation, 0.75-1 mM
Ca2+
-
slightly stimulates at 0.75-1 mM
Mg2+
-
activation, 0.75-1 mM
Zinc
-
zinc enzyme, 2.5 gatom zinc/62000 MW enzyme subunit, atomic absorption spectroscopy
Mg2+
-
slightly stimulates at 0.75-1 mM
additional information
-
the enzyme does not contain cobalt or manganese
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
0.2 mM, strong
2,2'-dipyridyl
-
2 mM
Alpha-macroglobulin
-
-
-
alpha2-Macroglobulin
-
-
-
Co2+
-
above 1-2 mM, native or apoenzyme
diethyldicarbonate
-
-
EDTA
-
inactivation by dialysis, 1-2 mM Zn2+, Mn2+ or Co2+ restores activity of metall-free apoenzyme to 0.5%, 10% and 50% of native enzyme, respectively, no restoring by Mg2+, Ca2+, Cu2+ or Fe3+; most effectively reversed by Co2+
EDTA
-
0.4 mM, partially reversed by Ca2+ or Mg2+
EGTA
-
about 25% as effective as EDTA or CDTA
Lectin from Canavalia ensiformis
-
not from Ricinus communis
-
p-chloromercuribenzoic acid
-
-
phosphoramidon
-
weak
phosphoramidon
-
inhibits at a high concentration
tosyl-Lys chloromethyl ketone
-
2 mM, less efficient than tosyl-Phe-chloromethyl ketone
tosyl-Phe chloromethyl ketone
-
i.e. TPCK, 2 mM
Zn2+
-
above 1-2 mM, native or apoenzyme
Mn2+
-
above 1-2 mM, native or apoenzyme
additional information
-
no inhibition by trypsin inhibitor, 6-aminohexanoic acid; pepstatin A
-
additional information
-
chymostatin, antipain, leupeptin; pepstatin A; various amino acids, protease inhibitor E-64
-
additional information
-
chymostatin, antipain, leupeptin; pepstatin A
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
11
-
about half-maximal activity at pH 6 and 11, about 80% of maximal activity at pH 7 and 10.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
mt+ (predominantly, ) and mt- gametes
Manually annotated by BRENDA team
additional information
-
mating gamete
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme, i.e. r-lysin, is released from periplasmic space during the first few min of mating
-
Manually annotated by BRENDA team
-
as inactive precursor molecule of higher MW, i.e. stored lysin or s-lysin; sexual signalling induces conversion to lower MW active enzyme and release, i.e. released lysin or r-lysin
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
49630
-
-
mature enzyme
60000
62000
-
active enzyme secreted into the mating medium
65000
-
-
proenzyme
67000
-
-
Chlamydomonas reinhardtii, gel filtration
additional information
-
-
each gamete mating type contains a single form of enzyme, the s-lysin of m+ is of slightly higher molecular mass than that of m-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 62000, Chlamydomonas reinhardtii, SDS-PAGE
?
-
x * 60000, Chlamydomonas reinhardtii, SDS-PAGE
monomer
-
1 * 67000, Chlamydomonas reinhardtii, SDS-PAGE
additional information
-
the enzyme is found as large aggregates with different molecular masses in culture medium or under low salt concentration, MW 120000, 180000, 220000 and higher
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9
-
-
several h stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
5 min; inactivation
50
-
-
30 min; inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DTT stabilizes
-
Freeze-thawing of cells releases substantial amounts of inactive s-lysin in a soluble form
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70°C, in Tris-acetate buffer, pH 7.5, 0.2 M NaCl, 2 mM DTT
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freeze-thawing of cells releases substantial amounts of inactive s-lysin in a soluble form
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
degradation
-
degrades gametic cell walls, cell walls of vegetative cells and those of mother sporangial cells