Literature summary extracted from

Krusong, K.; Ismail, A.; Wangpaiboon, K.; Pongsawasdi, P.
Production of large-ring cyclodextrins by amylomaltases (2022), Molecules, 27, 1446.

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
2.4.1.25	chloroplast	-	Arabidopsis thaliana	9507	-
2.4.1.25	chloroplast	-	Solanum tuberosum	9507	-
2.4.1.25	chloroplast	-	Oryza sativa Japonica Group	9507	-
2.4.1.25	cytosol	-	Arabidopsis thaliana	5829	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.25	Acidothermus cellulolyticus	A0LVB3	-	-
2.4.1.25	Acidothermus cellulolyticus 11B	A0LVB3	-	-
2.4.1.25	Acidothermus cellulolyticus ATCC 43068	A0LVB3	-	-
2.4.1.25	Acidothermus cellulolyticus DSM 8971	A0LVB3	-	-
2.4.1.25	Aquifex aeolicus	O66937	-	-
2.4.1.25	Arabidopsis thaliana	Q9LV91	-	-
2.4.1.25	Arabidopsis thaliana	Q8RXD9	-	-
2.4.1.25	Borreliella burgdorferi	A6YM39	-	-
2.4.1.25	Corynebacterium glutamicum	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum 534	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum ATCC 13032	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum BCRC 11384	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum CCUG 27702	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum DSM 20300	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum JCM 1318	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum LMG 3730	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum NBRC 12168	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum NCIMB 10025	Q8NNA7	-	-
2.4.1.25	Corynebacterium glutamicum NRRL B-2784	Q8NNA7	-	-
2.4.1.25	Escherichia coli	P15977	-	-
2.4.1.25	Escherichia coli K12	P15977	-	-
2.4.1.25	Manihot esculenta	A0A2C9VJ68	cv. AM560-2, Jatropha manihot	-
2.4.1.25	Manihot esculenta Crantz	A0A2C9VJ68	cv. AM560-2, Jatropha manihot	-
2.4.1.25	Oryza sativa Japonica Group	Q8LI30	-	-
2.4.1.25	Oryza sativa Japonica Group	Q69Q02	-	-
2.4.1.25	Pyrobaculum aerophilum	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum aerophilum ATCC 51768	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum aerophilum CIP 104966	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum aerophilum DSM 7523	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum aerophilum IM2	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum aerophilum JCM 9630	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum aerophilum NBRC 100827	Q8ZXM0	-	-
2.4.1.25	Pyrobaculum calidifontis	A3MU77	-	-
2.4.1.25	Pyrobaculum calidifontis DSM 21063	A3MU77	-	-
2.4.1.25	Pyrobaculum calidifontis JCM 11548	A3MU77	-	-
2.4.1.25	Pyrobaculum calidifontis VA1	A3MU77	-	-
2.4.1.25	Saccharophagus degradans	Q21M31	-	-
2.4.1.25	Saccharophagus degradans ATCC 43961	Q21M31	-	-
2.4.1.25	Saccharophagus degradans DSM 17024	Q21M31	-	-
2.4.1.25	Solanum tuberosum	Q06801	-	-
2.4.1.25	Streptococcus agalactiae	A0A0E1EIJ0	-	-
2.4.1.25	Streptococcus agalactiae YZ1605	A0A0E1EIJ0	-	-
2.4.1.25	Synechocystis sp. PCC 6803	P72785	-	-
2.4.1.25	Thermus aquaticus	Q6JHX9	-	-
2.4.1.25	Thermus aquaticus ATCC 33923	Q6JHX9	-	-
2.4.1.25	Thermus brockianus	Q2VJA0	-	-
2.4.1.25	Thermus filiformis	A0A0K0Q020	-	-
2.4.1.25	Thermus scotoductus	A0A430UEB1	-	-
2.4.1.25	Thermus thermophilus	O87172	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.4.1.25	Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan	cyclization mechanism of amylomaltase, and large-ring cyclodextrin production by amylomaltase overview	Thermus aquaticus	a
2.4.1.25	Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan	cyclization mechanism of amylomaltase AtDPE1, overview	Arabidopsis thaliana	a

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.4.1.25	2.9	-	pH 5.5-6.0, 75°C, disproportionation activity	Thermus aquaticus
2.4.1.25	5.84	-	pH 7.0, 45°C, disproportionation activity	Synechocystis sp. PCC 6803
2.4.1.25	21.8	44.3	pH 6.0, 30-45°C, disproportionation activity	Corynebacterium glutamicum
2.4.1.25	44.2	-	pH 6.6, 90°C, disproportionation activity	Aquifex aeolicus
2.4.1.25	47.5	-	pH 6.7, 45°C, disproportionation activity	Solanum tuberosum
2.4.1.25	54	-	pH 6.0, 40°C, disproportionation activity	Streptococcus agalactiae
2.4.1.25	159	-	pH 6.5, 60°C, disproportionation activity	Thermus filiformis
2.4.1.25	400	-	pH 5.5-6.3, 72-75°C, disproportionation activity	Thermus thermophilus
2.4.1.25	450	-	pH 6.7, 95°C, disproportionation activity	Pyrobaculum aerophilum
2.4.1.25	690	-	pH 6.9, 80°C, disproportionation activity	Pyrobaculum calidifontis
2.4.1.25	9400	-	pH 6.9, 28°C, disproportionation activity	Escherichia coli
2.4.1.25	17734	-	pH 6.0, 70°C, disproportionation activity	Thermus brockianus

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from amylose	Aquifex aeolicus	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP50 from pea starch	Streptococcus agalactiae	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from synthetic amylose	Thermus aquaticus	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP60 from pea starch	Thermus filiformis	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP24-DP284 from sucrose and of DP12-DP36 from corn starch	Synechocystis sp. PCC 6803	?	-	-
2.4.1.25	additional information	the enzyme AtDPE1 produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from potato amylose	Arabidopsis thaliana	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from potato amylose	Manihot esculenta	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP17 to over DP100 from synthetic amylose	Solanum tuberosum	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum ATCC 13032	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum DSM 20300	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum JCM 1318	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum LMG 3730	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum NCIMB 10025	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum BCRC 11384	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from potato amylose	Manihot esculenta Crantz	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum CCUG 27702	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum NBRC 12168	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum NRRL B-2784	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch	Corynebacterium glutamicum 534	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP50 from pea starch	Streptococcus agalactiae YZ1605	?	-	-
2.4.1.25	additional information	the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from synthetic amylose	Thermus aquaticus ATCC 33923	?	-	-

Subunits

EC Number	Subunits	Comment	Organism
2.4.1.25	dimer	the D-enzyme from Arabidopsis thaliana (AtDPE1) is present in a dimeric form	Arabidopsis thaliana
2.4.1.25	additional information	the three-dimensional structure of TaAM can be divided into two main domains, namely domain A and B. The subdomains B1, B2, and B3 are generated from insertion loops of (alpha,beta)8 barrel structure of domain A. Co-crystallization of TaAM with 34mer CA presents it as an asymmetric dimer. Domain structure, overview	Thermus aquaticus
2.4.1.25	additional information	the monomeric AtDPE1 possesses a long N-terminal part as a dimerization arm for engagement	Arabidopsis thaliana
2.4.1.25	additional information	isoform AtDPE2 specially contains two putative carbohydrate-binding modules (CBM20) at the N-terminus. In addition, the catalytic domain sequence is also divided into two parts as there is an insertion of 173 amino acid residues between the area of nucleophilic and acid/base-catalytic residues	Arabidopsis thaliana

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.1.25	4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic	-	Arabidopsis thaliana
2.4.1.25	4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic	-	Oryza sativa Japonica Group
2.4.1.25	4-alpha-glucanotransferase DPE2	-	Arabidopsis thaliana
2.4.1.25	4-alpha-glucanotransferase DPE2	-	Oryza sativa Japonica Group
2.4.1.25	4-alpha-glucanotransferase, chloroplastic/amyloplastic	-	Solanum tuberosum
2.4.1.25	4alphaGTase	-	Pyrobaculum aerophilum
2.4.1.25	4alphaGTase	-	Pyrobaculum calidifontis
2.4.1.25	4alphaGTase	-	Aquifex aeolicus
2.4.1.25	4alphaGTase	-	Corynebacterium glutamicum
2.4.1.25	4alphaGTase	-	Streptococcus agalactiae
2.4.1.25	4alphaGTase	-	Thermus aquaticus
2.4.1.25	4alphaGTase	-	Thermus filiformis
2.4.1.25	4alphaGTase	-	Thermus brockianus
2.4.1.25	4alphaGTase	-	Thermus thermophilus
2.4.1.25	4alphaGTase	-	Acidothermus cellulolyticus
2.4.1.25	4alphaGTase	-	Borreliella burgdorferi
2.4.1.25	4alphaGTase	-	Escherichia coli
2.4.1.25	4alphaGTase	-	Saccharophagus degradans
2.4.1.25	4alphaGTase	-	Synechocystis sp. PCC 6803
2.4.1.25	4alphaGTase	-	Thermus scotoductus
2.4.1.25	4alphaGTase	-	Arabidopsis thaliana
2.4.1.25	4alphaGTase	-	Manihot esculenta
2.4.1.25	4alphaGTase	-	Solanum tuberosum
2.4.1.25	4alphaGTase	-	Oryza sativa Japonica Group
2.4.1.25	amylomaltase	-	Pyrobaculum aerophilum
2.4.1.25	amylomaltase	-	Pyrobaculum calidifontis
2.4.1.25	amylomaltase	-	Aquifex aeolicus
2.4.1.25	amylomaltase	-	Corynebacterium glutamicum
2.4.1.25	amylomaltase	-	Streptococcus agalactiae
2.4.1.25	amylomaltase	-	Thermus aquaticus
2.4.1.25	amylomaltase	-	Thermus filiformis
2.4.1.25	amylomaltase	-	Thermus brockianus
2.4.1.25	amylomaltase	-	Thermus thermophilus
2.4.1.25	amylomaltase	-	Acidothermus cellulolyticus
2.4.1.25	amylomaltase	-	Borreliella burgdorferi
2.4.1.25	amylomaltase	-	Escherichia coli
2.4.1.25	amylomaltase	-	Saccharophagus degradans
2.4.1.25	amylomaltase	-	Synechocystis sp. PCC 6803
2.4.1.25	amylomaltase	-	Thermus scotoductus
2.4.1.25	amylomaltase	-	Arabidopsis thaliana
2.4.1.25	amylomaltase	-	Manihot esculenta
2.4.1.25	amylomaltase	-	Solanum tuberosum
2.4.1.25	amylomaltase	-	Oryza sativa Japonica Group
2.4.1.25	AtDPE1	-	Arabidopsis thaliana
2.4.1.25	AtDPE2	-	Arabidopsis thaliana
2.4.1.25	CgAM	-	Corynebacterium glutamicum
2.4.1.25	DPE1	-	Arabidopsis thaliana
2.4.1.25	DPE1	-	Oryza sativa Japonica Group
2.4.1.25	DPE2	-	Arabidopsis thaliana
2.4.1.25	DPE2	-	Oryza sativa Japonica Group
2.4.1.25	DPEP	-	Solanum tuberosum
2.4.1.25	MalQ	-	Pyrobaculum aerophilum
2.4.1.25	MalQ	-	Pyrobaculum calidifontis
2.4.1.25	MalQ	-	Aquifex aeolicus
2.4.1.25	MalQ	-	Corynebacterium glutamicum
2.4.1.25	MalQ	-	Streptococcus agalactiae
2.4.1.25	MalQ	-	Thermus aquaticus
2.4.1.25	MalQ	-	Thermus filiformis
2.4.1.25	MalQ	-	Thermus brockianus
2.4.1.25	MalQ	-	Thermus thermophilus
2.4.1.25	MalQ	-	Acidothermus cellulolyticus
2.4.1.25	MalQ	-	Borreliella burgdorferi
2.4.1.25	MalQ	-	Escherichia coli
2.4.1.25	MalQ	-	Saccharophagus degradans
2.4.1.25	MalQ	-	Synechocystis sp. PCC 6803
2.4.1.25	MalQ	-	Thermus scotoductus
2.4.1.25	MalQ	-	Arabidopsis thaliana
2.4.1.25	MalQ	-	Manihot esculenta
2.4.1.25	MalQ	-	Solanum tuberosum
2.4.1.25	MalQ	-	Oryza sativa Japonica Group
2.4.1.25	MeDPE1	-	Manihot esculenta
2.4.1.25	OsDPE1	-	Oryza sativa Japonica Group
2.4.1.25	OsDPE2	-	Oryza sativa Japonica Group
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Pyrobaculum aerophilum
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Pyrobaculum calidifontis
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Aquifex aeolicus
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Corynebacterium glutamicum
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Streptococcus agalactiae
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Thermus aquaticus
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Thermus filiformis
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Thermus brockianus
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Thermus thermophilus
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Acidothermus cellulolyticus
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Borreliella burgdorferi
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Escherichia coli
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Saccharophagus degradans
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Synechocystis sp. PCC 6803
2.4.1.25	prokaryotic 4-alpha-glucanotransferase	-	Thermus scotoductus
2.4.1.25	Sde_0986	-	Saccharophagus degradans
2.4.1.25	TaAM	-	Thermus aquaticus
2.4.1.25	TBGT	-	Thermus brockianus
2.4.1.25	TfAM	-	Thermus filiformis
2.4.1.25	TtAM	-	Thermus thermophilus

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.4.1.25	28	-	disproportionation activity	Escherichia coli
2.4.1.25	30	45	disproportionation and cyclization activity	Corynebacterium glutamicum
2.4.1.25	30	39	disproportionation activity	Oryza sativa Japonica Group
2.4.1.25	30	-	cyclization activity	Streptococcus agalactiae
2.4.1.25	35	-	disproportionation activity	Saccharophagus degradans
2.4.1.25	37	-	disproportionation activity	Arabidopsis thaliana
2.4.1.25	37	-	disproportionation activity	Borreliella burgdorferi
2.4.1.25	37	-	disproportionation activity	Manihot esculenta
2.4.1.25	40	-	disproportionation activity	Streptococcus agalactiae
2.4.1.25	42	-	disproportionation activity	Arabidopsis thaliana
2.4.1.25	45	-	disproportionation activity	Solanum tuberosum
2.4.1.25	45	-	disproportionation activity	Synechocystis sp. PCC 6803
2.4.1.25	60	-	disproportionation activity	Thermus filiformis
2.4.1.25	70	-	disproportionation activity	Thermus brockianus
2.4.1.25	70	-	cyclization activity	Thermus filiformis
2.4.1.25	72	75	disproportionation activity	Thermus thermophilus
2.4.1.25	75	-	disproportionation activity	Acidothermus cellulolyticus
2.4.1.25	75	-	disproportionation activity	Thermus aquaticus
2.4.1.25	75	-	disproportionation activity	Thermus scotoductus
2.4.1.25	80	-	disproportionation activity	Pyrobaculum calidifontis
2.4.1.25	90	-	disproportionation activity	Aquifex aeolicus
2.4.1.25	95	-	disproportionation activity	Pyrobaculum aerophilum

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.4.1.25	5	-	cyclization activity	Thermus filiformis
2.4.1.25	5.5	6	disproportionation activity	Thermus aquaticus
2.4.1.25	5.5	6.3	disproportionation activity	Thermus thermophilus
2.4.1.25	5.5	-	disproportionation activity	Borreliella burgdorferi
2.4.1.25	6	-	disproportionation and cyclization activity	Corynebacterium glutamicum
2.4.1.25	6	-	disproportionation and cyclization activities	Streptococcus agalactiae
2.4.1.25	6	-	disproportionation activity	Thermus brockianus
2.4.1.25	6	8	disproportionation activity	Arabidopsis thaliana
2.4.1.25	6	8	disproportionation activity	Manihot esculenta
2.4.1.25	6	7	disproportionation activity	Oryza sativa Japonica Group
2.4.1.25	6.5	-	disproportionation activity	Thermus filiformis
2.4.1.25	6.6	-	disproportionation activity	Aquifex aeolicus
2.4.1.25	6.7	-	disproportionation activity	Pyrobaculum aerophilum
2.4.1.25	6.7	-	disproportionation activity	Solanum tuberosum
2.4.1.25	6.9	-	disproportionation activity	Pyrobaculum calidifontis
2.4.1.25	6.9	-	disproportionation activity	Escherichia coli
2.4.1.25	7	-	disproportionation activity	Synechocystis sp. PCC 6803
2.4.1.25	7	-	disproportionation activity	Arabidopsis thaliana
2.4.1.25	7.5	-	disproportionation activity	Acidothermus cellulolyticus
2.4.1.25	7.5	-	disproportionation activity	Thermus scotoductus
2.4.1.25	8.5	-	disproportionation activity	Saccharophagus degradans

General Information

EC Number	General Information	Comment	Organism
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Pyrobaculum aerophilum
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Pyrobaculum calidifontis
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Aquifex aeolicus
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Corynebacterium glutamicum
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Streptococcus agalactiae
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Thermus aquaticus
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Thermus filiformis
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Thermus brockianus
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Thermus thermophilus
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Acidothermus cellulolyticus
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Borreliella burgdorferi
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Escherichia coli
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Saccharophagus degradans
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Synechocystis sp. PCC 6803
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Thermus scotoductus
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Arabidopsis thaliana
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Manihot esculenta
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Solanum tuberosum
2.4.1.25	evolution	members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77	Oryza sativa Japonica Group
2.4.1.25	additional information	the catalytic triad residues of TaAM consist of D293, E340, and D395 as a nucleophile, acid-base catalyst, and transition state-stabilizer, respectively. Structure-function analysis, overview	Thermus aquaticus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Pyrobaculum aerophilum
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Pyrobaculum calidifontis
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Aquifex aeolicus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Corynebacterium glutamicum
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Streptococcus agalactiae
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Thermus aquaticus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Thermus filiformis
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Thermus brockianus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Thermus thermophilus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Acidothermus cellulolyticus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Borreliella burgdorferi
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Escherichia coli
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Saccharophagus degradans
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Synechocystis sp. PCC 6803
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Thermus scotoductus
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Arabidopsis thaliana
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Manihot esculenta
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Solanum tuberosum
2.4.1.25	physiological function	4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes	Oryza sativa Japonica Group