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Information on EC 3.5.1.136 - N,N'-diacetylchitobiose non-reducing end deacetylase
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3.5.1.136 N,N'-diacetylchitobiose non-reducing end deacetylaseIUBMB Comments
The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N'-diacetylchitobiose, the end product of the archaeal chitinase, to produce beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N'-diacetylchitobiose at the reducing residue to produce N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine
+
Synonyms
CDA, Dac, diacetylchitobiose deacetylase, N,N'-diacetylchitobiose deacetylase, NAc2 deacetylase, PH0499, Tk-Dac, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CDA
-
-
-
-
Dac
diacetylchitobiose deacetylase
N,N'-diacetylchitobiose deacetylase
PH0499
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N'-diacetylchitobiose + H2O = beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
N,N'-diacetylchitobiose non-reducing end acetylhydrolase
The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N'-diacetylchitobiose, the end product of the archaeal chitinase, to produce beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N'-diacetylchitobiose at the reducing residue to produce N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
chitin degradation pathway in hyperthermophilic archaea
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
chitin degradation pathway in hyperthermophilic archaea
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the enzyme is involved in the chitin catabolic pathway
-
-
?
N-acetyl-D-glucosamine + H2O
beta-D-glucosamine + acetate
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
chitin degradation pathway in hyperthermophilic archaea
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
chitin degradation pathway in hyperthermophilic archaea
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
the enzyme is involved in the archaea-specific chitinolytic pathways by deacetylating the disaccharide end product of chitinase
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + acetate
the enzyme is involved in the chitin catabolic pathway
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the catalytic Zn2+ is situated at the end of the intermolecular cleft (which is formed by two polypeptides in the trimeric assembly) is coordinated by three side chain ligands from His44, Asp47, and His155, and by a phosphate ion derived from the crystallization reservoir solution
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
98
N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine
pH 8.0, 70°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0684
N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine
pH 8.0, 70°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 100
37°C: about 20% of maximal activity, 100°C: about 20% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). DCHI_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
267
0
30302
Swiss-Prot
-
O58235_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
272
0
31595
TrEMBL
-
Q8U3V1_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
267
0
31024
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homohexamer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, native enzyme and its selenomethionine derivative are crystallized and analyzed in the presence and absence of cadmium ion
hanging drop vapor-diffusion method at 20°C, crystal structure of the enzyme in complex with the inhibitor 2-deoxy-2-methylphosphoramido-D-glucose
hanging-drop vapor-diffusion method, the crystal structure is determined at resolutions of 2.0 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R157T
mutant enzyme exhibits much higher specific activity and catalytic efficiency as compared to wild-type enzyme
R157T
R157T
-
mutant enzyme exhibits much higher specific activity and catalytic efficiency as compared to wild-type enzyme
-
R157T
-
mutant enzyme exhibits much higher specific activity and catalytic efficiency as compared to wild-type enzyme
-
R157T
-
mutant enzyme exhibits much higher specific activity and catalytic efficiency as compared to wild-type enzyme
-
R157T
-
mutant enzyme exhibits much higher specific activity and catalytic efficiency as compared to wild-type enzyme
-
R157T
-
mutant enzyme exhibits much higher specific activity and catalytic efficiency as compared to wild-type enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified by polymerase chain reaction, cloned into expression vector pET15b, and expressed in E. coli BL21-codonPlus (DE3)-RIL
expression in Bacillus subtilis WB600 is better than expression in Escherichia coli BL21(DE3)
no expression in the soluble fraction of Escherichia coli harboring the expression plasmid. Insertion of the target genes into the chromosome of Escherichia coli yields the soluble recombinant protein
overexpressed as inclusion bodies in Escherichia coli Rosetta (DE3) pLys and successfully refolded in vitro
no expression in the soluble fraction of Escherichia coli harboring the expression plasmid. Insertion of the target genes into the chromosome of Escherichia coli yields the soluble recombinant protein
no expression in the soluble fraction of Escherichia coli harboring the expression plasmid. Insertion of the target genes into the chromosome of Escherichia coli yields the soluble recombinant protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is not observed under basal culture condition. It is induced by the addition of GlcNAc2. GlcNAc, lactose, cellobiose, maltose or GlcN can not act as an inducer
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
a whole-cell biocatalytic process for the environment-friendly synthesis of glucosamine is developed. Biotechnological production of GlcN in Bacillus subtilis is more environmentally friendly than the traditional multistep chemical synthesis approach. It has great a potential for large-scale production of GlcN in an environment-friendly manner
synthesis
production of chitosan oligosaccharides and monosaccharides
synthesis
-
production of chitosan oligosaccharides and monosaccharides
-
synthesis
-
production of chitosan oligosaccharides and monosaccharides
-
synthesis
-
production of chitosan oligosaccharides and monosaccharides
-
synthesis
-
production of chitosan oligosaccharides and monosaccharides
-
synthesis
-
production of chitosan oligosaccharides and monosaccharides
-
synthesis
Pyrococcus furiosus ATCC 700860
-
a whole-cell biocatalytic process for the environment-friendly synthesis of glucosamine is developed. Biotechnological production of GlcN in Bacillus subtilis is more environmentally friendly than the traditional multistep chemical synthesis approach. It has great a potential for large-scale production of GlcN in an environment-friendly manner
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakamura, T.; Yonezawa, Y.; Tsuchiya, Y.; Niiyama, M.; Ida, K.; Oshima, M.; Morita, J.; Uegaki, K.
Substrate recognition of N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii
J. Struct. Biol.
195
286-293
2016
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii ATCC 700860 (O58235)
brenda
Jiang, Z.; Niu, T.; Lv, X.; Liu, Y.; Li, J.; Lu, W.; Du, G.; Chen, J.; Liu, L.
Secretory expression fine-tuning and directed evolution of diacetylchitobiose deacetylase by Bacillus subtilis
Appl. Environ. Microbiol.
85
e01076-19
2019
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii ATCC 700860 (O58235)
brenda
Jiang, Z.; Lv, X.; Liu, Y.; Shin, H.D.; Li, J.; Du, G.; Liu, L.
Biocatalytic production of glucosamine from N-acetylglucosamine by diacetylchitobiose deacetylase
J. Microbiol. Biotechnol.
28
1850-1858
2018
Pyrococcus furiosus (Q8U3V1), Pyrococcus furiosus ATCC 700860 (Q8U3V1)
brenda
Nakamura, T.; Niiyama, M.; Hashimoto, W.; Ida, K.; Abe, M.; Morita, J.; Uegaki, K.
Multiple crystal forms of N,N'-diacetylchitobiose deacetylase from Pyrococcus furiosus
Acta Crystallogr. Sect. F
71
657-662
2015
Pyrococcus furiosus (Q8U3V1), Pyrococcus furiosus ATCC 43587 (Q8U3V1)
brenda
Mine, S.; Niiyama, M.; Hashimoto, W.; Ikegami, T.; Koma, D.; Ohmoto, T.; Fukuda, Y.; Inoue, T.; Abe, Y.; Ueda, T.; Morita, J.; Uegaki, K.; Nakamura, T.
Expression from engineered Escherichia coli chromosome and crystallographic study of archaeal N,N-diacetylchitobiose deacetylase
FEBS J.
281
2584-2596
2014
Pyrococcus horikoshii (O58235), Pyrococcus furiosus (Q8U3V1), Pyrococcus furiosus ATCC 43587 (Q8U3V1), Pyrococcus horikoshii ATCC 700860 (O58235)
brenda
Tanaka, T.; Fukui, T.; Fujiwara, S.; Atomi, H.; Imanaka, T.
Concerted action of diacetylchitobiose deacetylase and exo-beta-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
J. Biol. Chem.
279
30021-30027
2004
Thermococcus kodakarensis (Q6F4N1)
brenda
Mine, S.; Ikegami, T.; Kawasaki, K.; Nakamura, T.; Uegaki, K.
Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii
Protein Expr. Purif.
84
265-269
2012
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii ATCC 700860 (O58235)
brenda
Liu, B.; Ni, J.; Shen, Y.
Cloning, expression and biochemical characterization of a novel diacetylchitobiose deacetylase from the hyperthermophilic archaeon Pyrococcus horikoshii
Wei Sheng Wu Xue Bao
46
255-258
2006
Pyrococcus horikoshii (O58235), Pyrococcus horikoshii ATCC 700860 (O58235)
brenda
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Release 2023.1 (January 2023)
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