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Information on EC 3.4.24.38 - gametolysin
for references in articles please use BRENDA:EC3.4.24.38
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.38 gametolysin
IUBMB Comments
A glycoprotein found in the periplasmic space of Chlamydomonas reinhardtii gametes in a 62 kDa inactive form; decreased to 60 kDa upon activation. A zinc enzyme, inhibited by phosphoramidon, but also thiol activated. Type example of peptidase family M11
The expected taxonomic range for this enzyme is: Chlamydomonas reinhardtii
- 3.4.24.38
- autolysins
-
pneumococcal
-
mating-type
-
n-acetylmuramidase
- degradation
Reaction Schemes
showCleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-/-Arg-Phe-Ala
Synonyms
cell wall lytic enzyme, g-lysin, gametolysin, gamete lytic enzyme, gamete autolysin, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chlamydomonas cell wall degrading protease
-
-
-
-
Chlamydomonas reinhardtii metalloproteinase
-
-
-
-
Gamete lytic enzyme
Gametolysin
-
-
-
-
GLE
Gamete lytic enzyme
-
-
-
-
GLE
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
97089-74-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
fragments of azocasein
-
Substrates: poor substrate
Products: -
Products: -
?
casein + H2O
polypeptides derived from casein
-
Substrates: alpha- and beta-casein, poor substrate
Products: -
Products: -
?
Chlamydomonas cell wall polypeptide + H2O
?
-
Substrates: 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
Products: -
Products: -
?
Leu-Trp-Met-Arg-Phe-Ala + H2O
Leu-Trp-Met + Arg-Phe-Ala + Leu-Trp + Met-Arg-Phe-Ala
-
Substrates: -
Products: -
Products: -
?
Proteins rich in proline and hydroxyproline + H2O
?
-
Substrates: -
Products: -
Products: -
?
Cell wall protein + H2O
?
-
Substrates: cell wall lytic enzyme, reaction involved in cell fusion during mating of Chlamydomonas reinhardtii gametes
Products: -
Products: -
?
Cell wall protein + H2O
?
-
Substrates: released during agglutination of gametes of opposite mating type
Products: -
Products: -
?
Zoosporangia cell walls + H2O
?
-
Substrates: glutaraldehyde-fixed
Products: -
Products: -
?
Zoosporangia cell walls + H2O
?
-
Substrates: selected domains within walls of gametes, zoospores or zoosporangia
Products: -
Products: -
?
additional information
?
-
-
Substrates: bovine serum albumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: bovine serum albumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: insulin B-chain
Products: -
Products: -
?
additional information
?
-
-
Substrates: hemoglobin, casein, poly(Pro) or poly(hydroxyproline)
Products: -
Products: -
?
additional information
?
-
-
Substrates: Chlamydomonas reinhardtii has a second cell wall lytic enzyme, a sporangial autolysin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are cytochrome c, lysozyme, myoglobin, trypsin inhibitor, ovalbumin
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme activity is detected by chlorophyll release from cells
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: the enzyme activity is detected by chlorophyll release from cells
Products: -
Products: -
-
Cell wall protein + H2O
?
-
Substrates: cell wall lytic enzyme, reaction involved in cell fusion during mating of Chlamydomonas reinhardtii gametes
Products: -
Products: -
?
Cell wall protein + H2O
?
-
Substrates: released during agglutination of gametes of opposite mating type
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Zinc
-
zinc enzyme, 2.5 gatom zinc/62000 MW enzyme subunit, atomic absorption spectroscopy
additional information
-
the enzyme does not contain cobalt or manganese
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tosyl-Lys chloromethyl ketone
-
2 mM, less efficient than tosyl-Phe-chloromethyl ketone
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+
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
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
about half-maximal activity at pH 6 and 11, about 80% of maximal activity at pH 7 and 10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains CC-124, CC-125, CC-503, and CC-620/621
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
method development for enzyme production, proposal of a simple protocol for autolysin production requiring transfer of cells from plates into a dense liquid suspension, gametogenesis by overnight incubation before mixing of gametes, and enzyme harvesting after 2 h
brenda
additional information
additional information
-
mt+ (predominantly, ) and mt- gametes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme, i.e. r-lysin, is released from periplasmic space during the first few min of mating
-
brenda
the metalloprotease is released during sexual mating
-
brenda
-
as inactive precursor molecule of higher MW, i.e. stored lysin or s-lysin
-
brenda
-
sexual signalling induces conversion to lower MW active enzyme and release, i.e. released lysin or r-lysin
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
gametolysin treatment induces transcriptional activation of cell wall-related genes
physiological function
autolysin is produced by Chlamydomonas rheinhardtii during mating in order to digest the cell wall and allow cell fusion of two partners
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Freeze-thawing of cells releases substantial amounts of inactive s-lysin in a soluble form
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
freeze-thawing of cells releases substantial amounts of inactive s-lysin in a soluble form
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
degrades gametic cell walls, cell walls of vegetative cells and those of mother sporangial cells
molecular biology
autolysin is produced by Chlamydomonas rheinhardtii during mating in order to digest the cell wall and allow cell fusion of the two partners. Autolysin can be extracted from a mixture of mating cells by centrifugation, preserved by freezing at -80 C, and used later on any given walled strain to prepare for transformation. Development of a a very simple protocol that requires minimal monitoring of cell growth and density, with overall over 70% efficiency. This allows researchers interested in using the CRISPR technology to produce good quality autolysin and obtain mutated strains in their gene of interest, regardless of their favorite wild-type strain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsuda, Y.; Yamasaki, A.; Saito, T.; Yamaguchi, T.
Purification and characterization of cell wall lytic enzyme released by mating gametes of Chlamydomonas reinhardtii
FEBS Lett.
166
293-297
1984
Chlamydomonas reinhardtii
-
brenda
Matsuda, Y.; Saito, T.; Yamaguchi, T.; Kawase, H.
Cell wall lytic enzyme released by mating gametes of Chlamydomonas reinhardtii is a metalloprotease and digests the sodium perchlorate-insoluble component of cell wall
J. Biol. Chem.
260
6373-6377
1985
Chlamydomonas reinhardtii
brenda
Buchanan, M.J.; Imam, S.H.; Eskue, W.A.; Snell, W.J.
Activation of the cell wall degrading protease, lysin, during sexual signalling in Chlamydomonas: the enzyme is stored as an inactive, higher relative molecular mass precursor in the periplasm
J. Cell Biol.
108
199-207
1989
Chlamydomonas reinhardtii
brenda
Jaenicke, L.; Kuhne, W.; Spessert, R.; Wahle, U.; Waffenschmidt, S.
Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases
Eur. J. Biochem.
170
485-491
1987
Chlamydomonas reinhardtii
brenda
Matsuda, Y.; Saito, T.; Taketoshi, T.
Two novel endopeptidases released into the medium during mating of gametes of Chlamydomonas reinhardtii
Plant Cell Physiol.
35
957-961
1994
Chlamydomonas reinhardtii
brenda
Matsuda, Y.; Kubo, T.
Gametolysin
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
592-595
2004
Chlamydomonas reinhardtii
-
brenda
Cronmiller, E.; Toor, D.; Shao, N.C.; Kariyawasam, T.; Wang, M.H.; Lee, J.H.
Cell wall integrity signaling regulates cell wall-related gene expression in Chlamydomonas reinhardtii
Sci. Rep.
9
12204
2019
Chlamydomonas reinhardtii (P31178), Chlamydomonas reinhardtii
brenda
Findinier, J.
Autolysin production from Chlamydomonas reinhardtii
Bio Protoc.
13
e4705
2023
Chlamydomonas reinhardtii (P31178)
brenda
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