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amylose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
glycogen
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 14.6%
-
?
isomaltopentaose
?
WP_028992696
the carboxy-terminal region of a thermostable CITase from Thermoanaerobacter thermocopriae has the ability to produce long isomaltooligosaccharides. It synthesizes alpha-1,6 glucosyl products with over seven degrees of polymerization by an alpha-1,6 glucosyl transfer reaction from maltopentaose, isomaltopentaose, or commercialized maltodextrins as substrates
-
-
?
maltodextrin
?
WP_028992696
the carboxy-terminal region of a thermostable CITase from Thermoanaerobacter thermocopriae has the ability to produce long isomaltooligosaccharides. It synthesizes alpha-1,6 glucosyl products with over seven degrees of polymerization by an alpha-1,6 glucosyl transfer reaction from maltopentaose, isomaltopentaose, or commercialized maltodextrins as substrates
-
-
?
maltoheptaose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 15.8%
-
?
maltohexaose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 12.7%
-
?
maltopentaose
?
WP_028992696
the carboxy-terminal region of a thermostable CITase from Thermoanaerobacter thermocopriae has the ability to produce long isomaltooligosaccharides. It synthesizes alpha-1,6 glucosyl products with over seven degrees of polymerization by an alpha-1,6 glucosyl transfer reaction from maltopentaose, isomaltopentaose, or commercialized maltodextrins as substrates
-
-
?
maltopentaose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 8.9%
-
?
maltotetraose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 4.3%
-
?
maltotriose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
poor substrate
yield 0.9%
-
?
partially hydrolyzed starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
soluble starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
soluble starch
cyclomaltooctaose
starch
?
key enzyme to synthesize alpha-(1->6)-glucan for cycloisomaltooligosaccharide production in dextran-free environments
-
-
?
starch
cycloisomaltooligosaccharide
the enzyme has a strong alpha-(1->4) to alpha-(1->6) transglucosylation activity. The enzyme exhibits higher hydrolysis activity against alpha-(1->4)-linked glucan than against alpha-(1->6)-linked glucan. It elongates alpha-(1->6)-linked glucooligosaccharide to at least a degree of polymerization of 10 through a successive transglucosylation reaction
-
-
?
additional information
?
-
amylose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 27.2%
-
?
amylose
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 27.2%
-
?
dextran
?
-
-
-
?
dextran
?
-
-
synthesis of seven- to nine-glucose-membered cycloisomaltooligosaccharides
-
?
dextran
?
-
-
synthesis of seven- to nine-glucose-membered cycloisomaltooligosaccharides
-
?
dextran
?
WP_028992696
cycloisomaltooligosaccharide-7 to cycloisomaltooligosaccharide-20 are mainly produced, with CI-7 as the main product
-
-
?
partially hydrolyzed starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
i.e. Pinedex no. 1, dextrose equivalent
yield 13.9%
-
?
partially hydrolyzed starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
i.e. Pinedex no. 100, dextrose equivalent 2 to 5
yield 201%
-
?
partially hydrolyzed starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
i.e. Pinedex no. 1, dextrose equivalent
yield 13.9%
-
?
partially hydrolyzed starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
i.e. Pinedex no. 100, dextrose equivalent 2 to 5
yield 201%
-
?
soluble starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
-
?
soluble starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 25.9%, optimization of production parameters
-
?
soluble starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 26.5%
-
?
soluble starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
yield 25.9%, optimization of production parameters
-
?
soluble starch
cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
-
-
-
?
soluble starch
cyclomaltooctaose
-
main product
-
?
soluble starch
cyclomaltooctaose
-
main product
-
?
additional information
?
-
-
enzyme acts on maltooligosaccharides that have degrees of polymerization of 3 or more, amylose, and soluble starch, to produce cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) by an intramolecular alpha-1,6-glycosyl transfer reaction. Enzyme additionally catalyzes the transfer of part of a linear oligosaccharide to another oligosaccharide by an intermolecular alpha-1,4-glycosyl transfer reaction
-
-
?
additional information
?
-
CITase catalyzes the synthesis of cycloisomaltooligosaccharides with 7-17 glucose units from dextran
-
-
?
additional information
?
-
isomaltotetraose is the smallest substrate for the CITase, and major product of recombinant CITase-T3040 is cycloisomaltooctaose
-
-
?
additional information
?
-
carbohydrate-binding module CBM35 functions in determining the size of the product, causing the predominant production of cycloisomaltooctaose by the enzyme. The isomaltoheptaose and cycloisomaltooctaose bind in the catalytic cleft with a circular structure around Met-310, representing the enzyme-product complex. The canonical sugar-binding site of CBM35 binds the mid-part of isomaltooligosaccharides
-
-
?
additional information
?
-
CITase from Bacillus circulans T-3040 produces mainly cycloisomaltooligosaccharides of 8 units with little megalo-cycloisomaltooligosaccharides with 10-12 glucose units
-
-
?
additional information
?
-
CITase catalyzes the synthesis of cycloisomaltooligosaccharides with 7-17 glucose units from dextran
-
-
?
additional information
?
-
CITase from Bacillus circulans T-3040 produces mainly cycloisomaltooligosaccharides of 8 units with little megalo-cycloisomaltooligosaccharides with 10-12 glucose units
-
-
?
additional information
?
-
carbohydrate-binding module CBM35 functions in determining the size of the product, causing the predominant production of cycloisomaltooctaose by the enzyme. The isomaltoheptaose and cycloisomaltooctaose bind in the catalytic cleft with a circular structure around Met-310, representing the enzyme-product complex. The canonical sugar-binding site of CBM35 binds the mid-part of isomaltooligosaccharides
-
-
?
additional information
?
-
isomaltotetraose is the smallest substrate for the CITase, and major product of recombinant CITase-T3040 is cycloisomaltooctaose
-
-
?
additional information
?
-
isomaltotetraose is the smallest substrate for the CITase, and major product of recombinant CITase-598K is cycloisomaltoheptaose
-
-
?
additional information
?
-
the enzyme displays extremely low activity against 4-nitrophenyl alpha-glucopyranoside. It does not display any hydrolytic activity against 4-nitrophenyl alpha-mannopyranoside, 4-nitrophenyl alpha-galactopyranoside, and 4-nitrophenyl alpha-xylopyranoside
-
-
-
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additional information
catalytically important residues of CITase-598K are Asp144, Asp269, and Glu341
evolution
CITase belongs to glycoside hydrolase family 66, GH6
evolution
CITase is a member of the glycoside hydrolase family 66, GH66
evolution
CITase is a member of the glycoside hydrolase family 66, GH66
evolution
-
CITase belongs to glycoside hydrolase family 66, GH6
-
evolution
-
CITase is a member of the glycoside hydrolase family 66, GH66
-
malfunction
15 deletion mutant enzymes. M123DELTA (R4-deleted), MDELTA234 (R1-deleted), and MDELTA23DELTA (R1/R4-deleted) catalyze cycloisomaltooligosaccharide synthesis, but other mutants are inactive. M123DELTA, MDELTA234, and MDELTA23DELTA increase their Km values against dextran 40. The wild-type enzyme and M123DELTA produced cycloisomaltooligosaccharide-8 predominantly, but MDELTA234 and MDELTA23DELTA lose cycloisomaltooligosaccharide-8 production specificity. The kcat values of MDELTA234 and MDELTA23DELTA decrease, and these mutants show narrowed temperature and pH stability ranges
malfunction
-
15 deletion mutant enzymes. M123DELTA (R4-deleted), MDELTA234 (R1-deleted), and MDELTA23DELTA (R1/R4-deleted) catalyze cycloisomaltooligosaccharide synthesis, but other mutants are inactive. M123DELTA, MDELTA234, and MDELTA23DELTA increase their Km values against dextran 40. The wild-type enzyme and M123DELTA produced cycloisomaltooligosaccharide-8 predominantly, but MDELTA234 and MDELTA23DELTA lose cycloisomaltooligosaccharide-8 production specificity. The kcat values of MDELTA234 and MDELTA23DELTA decrease, and these mutants show narrowed temperature and pH stability ranges
-
physiological function
CITase production is induced by dextran 40, isomaltose, isomaltotriose, and panose, and soluble starch but not by G67 or dextrin, which suggests that alpha-1,6 glucosidic linkages are required for CITase induction. Although CITase is induced by isomaltose, isomaltotriose, and panose, no cyclodextrans are produced in the culture. Cyclodextran-producing activity in the presence of soluble starch as the substrate is observed only in cultures containing dextran 40 or soluble starch. The production of CITase is significantly unaffected by glucose addition, but soluble starch-CITase activity almost completely disappears after glucose addition. A 135-kDa protein contributes to cyclodextran formation from starch in the presence of CITase
physiological function
-
CITase production is induced by dextran 40, isomaltose, isomaltotriose, and panose, and soluble starch but not by G67 or dextrin, which suggests that alpha-1,6 glucosidic linkages are required for CITase induction. Although CITase is induced by isomaltose, isomaltotriose, and panose, no cyclodextrans are produced in the culture. Cyclodextran-producing activity in the presence of soluble starch as the substrate is observed only in cultures containing dextran 40 or soluble starch. The production of CITase is significantly unaffected by glucose addition, but soluble starch-CITase activity almost completely disappears after glucose addition. A 135-kDa protein contributes to cyclodextran formation from starch in the presence of CITase
-
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A452N
-
3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
F268V/D469Y/A513V/Y515S
mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain
V744L
-
2fold increase in reaction velocity, 3fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
A452N
-
3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
-
F268V/D469Y/A513V/Y515S
-
mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain
-
V744L
-
2fold increase in reaction velocity, 3fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
-
D144A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D144N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D264A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D269A
site-directed mutagenesis, the mutant is inactive
D269N
site-directed mutagenesis, the mutant is almost inactive
D662A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E341A
site-directed mutagenesis, the mutant is inactive
E341Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
construction of CITase deletion mutants, 15 deletion mutant enzymes. M123DELTA (R4-deleted), MDELTA234 (R1-deleted), and MDELTA23DELTA (R1/R4-deleted) catalyze cycloisomaltooligosaccharide synthesis, but other mutants are inactive. M123DELTA, MDELTA234, and MDELTA23DELTA increase their Km values against dextran 40. The wild-type enzyme and M123DELTA produced cycloisomaltooligosaccharide-8 predominantly, but MDELTA234 and MDELTA23DELTA lose cycloisomaltooligosaccharide-8 production specificity. The kcat values of MDELTA234 and MDELTA23DELTA decrease, and these mutants show narrowed temperature and pH stability ranges, product size distribution of mutants, overview
additional information
utational studies show that substrate-binding sites B-1 and B-2 contribute to recruiting substrate and maintaining product size respectively
additional information
-
construction of CITase deletion mutants, 15 deletion mutant enzymes. M123DELTA (R4-deleted), MDELTA234 (R1-deleted), and MDELTA23DELTA (R1/R4-deleted) catalyze cycloisomaltooligosaccharide synthesis, but other mutants are inactive. M123DELTA, MDELTA234, and MDELTA23DELTA increase their Km values against dextran 40. The wild-type enzyme and M123DELTA produced cycloisomaltooligosaccharide-8 predominantly, but MDELTA234 and MDELTA23DELTA lose cycloisomaltooligosaccharide-8 production specificity. The kcat values of MDELTA234 and MDELTA23DELTA decrease, and these mutants show narrowed temperature and pH stability ranges, product size distribution of mutants, overview
-
additional information
-
utational studies show that substrate-binding sites B-1 and B-2 contribute to recruiting substrate and maintaining product size respectively
-
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Kawamoto, H.; Oguma, T.; Sekine, H.; Kobayashi, M.
Utilization of NaCl to suppress the growth of contaminating microbes during the continuous production of cycloisomaltooligosaccharides by immobilized enzyme
Biochem. Eng. J.
12
161-164
2002
Niallia circulans
-
brenda
Watanabe, H.; Nishimoto, T.; Kubota, M.; Chaen, H.; Fukuda, S.
Cloning, sequencing, and expression of the genes encoding an isocyclomaltooligosaccharide glucanotransferase and an alpha -amylase from a Bacillus circulans strain
Biosci. Biotechnol. Biochem.
70
2690-2702
2006
Niallia circulans (A0P8W9), Niallia circulans
brenda
Watanabe, H.; Takakura-Yamamoto, R.; Kurose, M.; Yoshida, K.; Oku, K.; Sawatani, I.; Nishimoto, T.; Kubota, M.; Chaen, H.; Fukuda, S.
Production of isocyclomaltopentaose from starch using isocyclomaltooligosaccharide glucanotransferase
Biosci. Biotechnol. Biochem.
70
3013-3018
2006
Niallia circulans, Niallia circulans AM7
brenda
Kawakita, H.; Sugita, K.; Saito, K.; Tamada, M.; Sugo, T.; Kawamoto, H.
Production of cycloisomaltooligosaccharides from dextran using enzyme immobilized in multilayers onto porous membranes
Biotechnol. Prog.
18
465-469
2002
Niallia circulans, Niallia circulans T-3040
brenda
Kawamoto, H.; Oguma, T.; Sekine, H.; Kobayashi, M.
Immobilization of cycloisomaltooligosaccharide glucanotransferase for the production of cycloisomaltooligosaccharides from dextran
Enzyme Microb. Technol.
28
515-521
2001
Niallia circulans
brenda
Funane, K.; Nakai, S.; Terasawa, K.; Oguma, T.; Kawamoto, H.; Kitamura, Y.; Kobayashi, M.
Mutation of Bacillus cyclodextran glucanotransferase to increase its reaction velocity
J. Appl. Glycosci.
50
33-35
2003
Niallia circulans, Niallia circulans T-3040
-
brenda
Watanabe, H.; Nishimoto, T.; Chaen, H.; Fukuda, S.
A novel glucanotransferase that produces a cyclomaltopentaose cyclized by an alpha-1,6-linkage
J. Appl. Glycosci.
54
109-118
2007
Niallia circulans
-
brenda
Kawabata, Y.; Kimura, K.; Funane, K.
Extracellular production of cycloisomaltooligosaccharide glucanotransferase and cyclodextran by a protease-deficient Bacillus subtilis host-vector system
Appl. Microbiol. Biotechnol.
93
1877-1884
2012
Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Funane, K.; Kawabata, Y.; Suzuki, R.; Kim, Y.M.; Kang, H.K.; Suzuki, N.; Fujimoto, Z.; Kimura, A.; Kobayashi, M.
Deletion analysis of regions at the C-terminal part of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040
Biochim. Biophys. Acta
1814
428-434
2011
Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Suzuki, R.; Terasawa, K.; Kimura, K.; Fujimoto, Z.; Momma, M.; Kobayashi, M.; Kimura, A.; Funane, K.
Biochemical characterization of a novel cycloisomaltooligosaccharide glucanotransferase from Paenibacillus sp. 598K
Biochim. Biophys. Acta
1824
919-924
2012
Paenibacillus sp. (G9MBW2), Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Suzuki, N.; Kim, Y.M.; Momma, M.; Fujimoto, Z.; Kobayashi, M.; Kimura, A.; Funane, K.
Crystallization and preliminary X-ray crystallographic analysis of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040
Acta Crystallogr. Sect. F
69
946-949
2013
Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Funane, K.; Ichinose, H.; Araki, M.; Suzuki, R.; Kimura, K.; Fujimoto, Z.; Kobayashi, M.; Kimura, A.
Evidence for cycloisomaltooligosaccharide production from starch by Bacillus circulans T-3040
Appl. Microbiol. Biotechnol.
98
3947-3954
2014
Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Suzuki, R.; Suzuki, N.; Fujimoto, Z.; Momma, M.; Kimura, K.; Kitamura, S.; Kimura, A.; Funane, K.
Molecular engineering of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040: structural determinants for the reaction product size and reactivity
Biochem. J.
467
259-270
2015
Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Suzuki, N.; Fujimoto, Z.; Kim, Y.M.; Momma, M.; Kishine, N.; Suzuki, R.; Suzuki, S.; Kitamura, S.; Kobayashi, M.; Kimura, A.; Funane, K.
Structural elucidation of the cyclization mechanism of alpha-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase
J. Biol. Chem.
289
12040-12051
2014
Niallia circulans (P94286), Niallia circulans T-3040 (P94286)
brenda
Ichinose, H.; Suzuki, R.; Miyazaki, T.; Kimura, K.; Momma, M.; Suzuki, N.; Fujimoto, Z.; Kimura, A.; Funane, K.
Paenibacillus sp. 598K 6-alpha-glucosyltransferase is essential for cycloisomaltooligosaccharide synthesis from alpha-(1->4)-glucan
Appl. Microbiol. Biotechnol.
101
4115-4128
2017
Paenibacillus sp. 598K (G9MBW2)
brenda
Fujimoto, Z.; Kishine, N.; Suzuki, N.; Suzuki, R.; Mizushima, D.; Momma, M.; Kimura, K.; Funane, K.
Isomaltooligosaccharide-binding structure of Paenibacillus sp. 598K cycloisomaltooligosaccharide glucanotransferase
Biosci. Rep.
37
BSR20170253
2017
Paenibacillus sp. 598K (G9MBW2)
brenda
Yang, S.J.; Choi, S.J.; Park, B.R.; Kim, Y.M.
Thermostable CITase from Thermoanaerobacter thermocopriae shows negative cooperativity
Biotechnol. Lett.
41
625-632
2019
Thermoanaerobacter thermocopriae (WP_028992696), Thermoanaerobacter thermocopriae
brenda
Jeong, W.S.; Lee, Y.R.; Hong, S.J.; Choi, S.J.; Choi, J.H.; Park, S.Y.; Woo, E.J.; Kim, Y.M.; Park, B.R.
Carboxy-terminal region of a thermostable CITase from Thermoanaerobacter thermocopriae has the ability to produce long isomaltooligosaccharides
J. Microbiol. Biotechnol.
29
1938-1946
2019
Thermoanaerobacter thermocopriae (WP_028992696), Thermoanaerobacter thermocopriae
brenda