Literature summary for 3.5.1.105 extracted from

Kaczmarek, M.; Struszczyk-Swita, K.; Li, X.; Szczesna-Antczak, M.; Daroch, M.
Enzymatic modifications of chitin, chitosan, and chitooligosaccharides (2019), Front. Bioeng. Biotechnol., 7, 243 .

Search for more literature for 3.5.1.105

Application

Application	Comment	Organism
synthesis	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Shewanella baltica
synthesis	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Puccinia graminis f. sp. tritici
synthesis	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Vibrio cholerae serotype O1

Protein Variants

Protein Variants	Comment	Organism
additional information	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Shewanella baltica
additional information	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Puccinia graminis f. sp. tritici
additional information	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Vibrio cholerae serotype O1

Organism

Organism	UniProt	Comment	Textmining
Puccinia graminis f. sp. tritici	E3K3D7	-	-
Puccinia graminis f. sp. tritici CRL 75-36-700-3	E3K3D7	-	-
Puccinia graminis f. sp. tritici race SCCL	E3K3D7	-	-
Shewanella baltica	A3D2G6	-	-
Shewanella baltica ATCC BAA-1091	A3D2G6	-	-
Shewanella baltica OS155	A3D2G6	-	-
Vibrio cholerae serotype O1	Q9KSH6	-	-
Vibrio cholerae serotype O1 ATCC 39315	Q9KSH6	-	-
Vibrio cholerae serotype O1 El Tor Inaba N16961	Q9KSH6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	activity increases with decreasing DP	Vibrio cholerae serotype O1	?	-	?
additional information	activity increases with increasing DP	Puccinia graminis f. sp. tritici	?	-	?
additional information	increase in activity DP2 > DP4 > DP3, product analysis	Shewanella baltica	?	-	?
additional information	activity increases with decreasing DP	Vibrio cholerae serotype O1 El Tor Inaba N16961	?	-	?
additional information	activity increases with increasing DP	Puccinia graminis f. sp. tritici race SCCL	?	-	?
additional information	increase in activity DP2 > DP4 > DP3, product analysis	Shewanella baltica OS155	?	-	?
additional information	activity increases with increasing DP	Puccinia graminis f. sp. tritici CRL 75-36-700-3	?	-	?
additional information	increase in activity DP2 > DP4 > DP3, product analysis	Shewanella baltica ATCC BAA-1091	?	-	?
additional information	activity increases with decreasing DP	Vibrio cholerae serotype O1 ATCC 39315	?	-	?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O	-	Puccinia graminis f. sp. tritici	?	-	?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O	-	Vibrio cholerae serotype O1	?	-	?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O	-	Puccinia graminis f. sp. tritici race SCCL	?	-	?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O	-	Puccinia graminis f. sp. tritici CRL 75-36-700-3	?	-	?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O	-	Puccinia graminis f. sp. tritici	?	-	?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O	-	Vibrio cholerae serotype O1	?	-	?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O	-	Vibrio cholerae serotype O1 El Tor Inaba N16961	?	-	?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O	-	Puccinia graminis f. sp. tritici race SCCL	?	-	?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O	-	Puccinia graminis f. sp. tritici CRL 75-36-700-3	?	-	?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O	-	Vibrio cholerae serotype O1 ATCC 39315	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Shewanella baltica	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Puccinia graminis f. sp. tritici	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Vibrio cholerae serotype O1	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Vibrio cholerae serotype O1 El Tor Inaba N16961	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Puccinia graminis f. sp. tritici race SCCL	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Shewanella baltica OS155	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Puccinia graminis f. sp. tritici CRL 75-36-700-3	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Shewanella baltica ATCC BAA-1091	?	-	?
N,N',N'',N'''-tetraacetylchitotetraose + H2O	-	Vibrio cholerae serotype O1 ATCC 39315	?	-	?
N,N',N''-triacetylchitotriose + H2O	-	Shewanella baltica	?	-	?
N,N',N''-triacetylchitotriose + H2O	-	Vibrio cholerae serotype O1	?	-	?
N,N',N''-triacetylchitotriose + H2O	-	Vibrio cholerae serotype O1 El Tor Inaba N16961	?	-	?
N,N',N''-triacetylchitotriose + H2O	-	Shewanella baltica OS155	?	-	?
N,N',N''-triacetylchitotriose + H2O	-	Shewanella baltica ATCC BAA-1091	?	-	?
N,N',N''-triacetylchitotriose + H2O	-	Vibrio cholerae serotype O1 ATCC 39315	?	-	?
N,N'-diacetylchitobiose + H2O	preferred substrate	Shewanella baltica	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	preferred substrate	Vibrio cholerae serotype O1	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	preferred substrate	Vibrio cholerae serotype O1 El Tor Inaba N16961	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	preferred substrate	Shewanella baltica OS155	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	preferred substrate	Shewanella baltica ATCC BAA-1091	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	preferred substrate	Vibrio cholerae serotype O1 ATCC 39315	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?

Synonyms

Synonyms	Comment	Organism
chitooligosaccharide deacetylase	-	Shewanella baltica
chitooligosaccharide deacetylase	-	Puccinia graminis f. sp. tritici
chitooligosaccharide deacetylase	-	Vibrio cholerae serotype O1
codA	-	Shewanella baltica
codA	-	Puccinia graminis f. sp. tritici
codA	-	Vibrio cholerae serotype O1
NodB homology domain-containing protein	UniProt	Puccinia graminis f. sp. tritici
NodB homology domain-containing protein	UniProt	Vibrio cholerae serotype O1
PGTG_04950	-	Puccinia graminis f. sp. tritici
polysaccharide deacetylase	UniProt	Shewanella baltica
Sbal_1411	-	Shewanella baltica
VC_1280	-	Vibrio cholerae serotype O1

General Information

General Information	Comment	Organism
evolution	chitin deacetylases and chitooligosaccharides deacetylases [EC 3.5.1.105 (CODa)]. ChDas and CODa are a group of enzymes catalyzing the hydrolysis of acetamido groups of N-acetyl-D-glucosamine residues in chitin, chitosan and chitooligosaccharides, respectively. Both of these groups of enzymes are classified in the carbohydrate esterase family 4 (CE4) in the CAZY database	Shewanella baltica
evolution	chitin deacetylases and chitooligosaccharides deacetylases [EC 3.5.1.105 (CODa)]. ChDas and CODa are a group of enzymes catalyzing the hydrolysis of acetamido groups of N-acetyl-D-glucosamine residues in chitin, chitosan and chitooligosaccharides, respectively. Both of these groups of enzymes are classified in the carbohydrate esterase family 4 (CE4) in the CAZY database	Puccinia graminis f. sp. tritici
evolution	chitin deacetylases and chitooligosaccharides deacetylases [EC 3.5.1.105 (CODa)]. ChDas and CODa are a group of enzymes catalyzing the hydrolysis of acetamido groups of N-acetyl-D-glucosamine residues in chitin, chitosan and chitooligosaccharides, respectively. Both of these groups of enzymes are classified in the carbohydrate esterase family 4 (CE4) in the CAZY database	Vibrio cholerae serotype O1
additional information	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Shewanella baltica
additional information	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Puccinia graminis f. sp. tritici
additional information	biotransformation of chitin into chitosan through enzymatic deacetylation can be achieved with chitin deacetylases (EC 3.5.1.41, ChDa). Other enzymes involved in chitin and chitosan conversion are chitinases (EC 3.2.1.14) and chitosanases (EC 3.2.1.132). Both of them catalyze the hydrolysis of glycosidic bonds but differ in substrate specificity, hydrolysing bonds of chitin and chitosan, respectively. Obtained chitooligosaccharides can be further enzymatically modified by chitooligosaccharides deacetylases (EC 3.5.1.105, CODa) to obtain products with desired chain arrangement	Vibrio cholerae serotype O1
physiological function	CODa isolated from different sources exhibit different catalytic mechanisms, indicating that a variety of well-defined chitooligosaccharides can be produced during a single enzymatic reaction	Shewanella baltica
physiological function	CODa isolated from different sources exhibit different catalytic mechanisms, indicating that a variety of well-defined chitooligosaccharides can be produced during a single enzymatic reaction	Puccinia graminis f. sp. tritici
physiological function	CODa isolated from different sources exhibit different catalytic mechanisms, indicating that a variety of well-defined chitooligosaccharides can be produced during a single enzymatic reaction	Vibrio cholerae serotype O1