EC 1.1.1.173     
Accepted name: L-rhamnose 1-dehydrogenase
Reaction: L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
Systematic name: L-rhamnofuranose:NAD+ 1-oxidoreductase
References:
1.  Rigo, L.U., Maréchal, L.R., Vieira, M.M. and Veiga, L.A. Oxidative pathway for L-rhamnose degradation in Pallularia pullulans. Can. J. Microbiol. 31 (1985) 817–822.
2.  Rigo, L.U., Nakano, M., Veiga, L.A. and Feingold, D.S. L-Rhamnose dehydrogenase of Pullularia pullulans. Biochim. Biophys. Acta 445 (1976) 286–293. [PMID: 8142]
[EC 1.1.1.173 created 1978]
 
 
EC 2.4.1.248     
Accepted name: cycloisomaltooligosaccharide glucanotransferase
Reaction: cyclizes part of a (1→6)-α-D-glucan chain by formation of a (1→6)-α-D-glucosidic bond
Systematic name: (1→6)-α-D-glucan:(1→6)-α-D-glucan 6-α-D-[1→6α-D-glucano]-transferase (cyclizing)
Comments: Specific for (1→6)-α-D-glucans (dextrans) and, unlike cyclomaltodextrin glucanotransferase (EC 2.4.1.19), without activity towards (1→4)-α-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1→6)-α-D-glucosidic linkages at branch points. The enzyme from Bacillus circulans T-3040 has been shown to form cycloisomalto-oligosaccharides of three sizes (7, 8 and 9 glucose units). It will also catalyse the disproportionation of two isomalto-oligosaccharides molecules to yield a series of isomalto-oligosachharides and the addition of D-glucose to cycloisomalto-oligosaccharides with ring opening to form isomalto-oligosaccharides.
References:
1.  Oguma T, Horiuchi, T, and Kobayashi M. Novel Cyclic dextrins, Cycloisomaltooligosaccharides, from Bacillus sp. T-3040 culture. Biosci. Biotech. Biochem. 57 (1993) 1225–1227.
2.  Oguma, T., Tobe, K. and Kobayashi, M. Purification and properties of a novel enzyme from Bacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosaccharides. FEBS Lett. 345 (1994) 135–138. [PMID: 7515357]
3.  Yamamoto, T., Terasawa, K., Kim, Y.M., Kimura, A., Kitamura, Y., Kobayashi, M. and Funane, K. Identification of catalytic amino acids of cyclodextran glucanotransferase from Bacillus circulans T-3040. Biosci. Biotechnol. Biochem. 70 (2006) 1947–1953. [PMID: 16926507]
[EC 2.4.1.248 created 2009]
 
 
EC 3.1.1.65     
Accepted name: L-rhamnono-1,4-lactonase
Reaction: L-rhamnono-1,4-lactone + H2O = L-rhamnonate
Other name(s): L-rhamno-γ-lactonase; L-rhamnono-γ-lactonase; L-rhamnonate dehydratase
Systematic name: L-rhamnono-1,4-lactone lactonohydrolase
References:
1.  Rigo, L.U., Maréchal, L.R., Vieira, M.M. and Veiga, L.A. Oxidative pathway for L-rhamnose degradation in Pallularia pullulans. Can. J. Microbiol. 31 (1985) 817–822.
[EC 3.1.1.65 created 1989]
 
 
EC 3.2.1.10     
Accepted name: oligo-1,6-glucosidase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (α-amylase), and in isomaltose
Other name(s): limit dextrinase (erroneous); isomaltase; sucrase-isomaltase; exo-oligo-1,6-glucosidase; dextrin 6α-glucanohydrolase; α-limit dextrinase; dextrin 6-glucanohydrolase; oligosaccharide α-1,6-glucohydrolase; α-methylglucosidase
Systematic name: oligosaccharide 6-α-glucohydrolase
Comments: This enzyme, like EC 3.2.1.33 (amylo-α-1,6-glucosidase), can release an α-1→6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose α-glucosidase). Differs from EC 3.2.1.33 (amylo-α-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
References:
1.  Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA 76 (1979) 5183–5186. [PMID: 291933]
2.  Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem. 255 (1980) 11332–11338. [PMID: 7002920]
3.  Rodriguez, I.R., Taravel, F.R. and Whelan, W.J. Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits. Eur. J. Biochem. 143 (1984) 575–582. [PMID: 6479163]
4.  Khan, N.A. and Eaton, N.R. Purification and characterization of maltase and α-methyl glucosidase from yeast. Biochim. Biophys. Acta 146 (1967) 173–180. [PMID: 6060462]
5.  Yamamoto, K., Nakayama, A., Yamamoto, Y. and Tabata, S. Val216 decides the substrate specificity of α-glucosidase in Saccharomyces cerevisiae. Eur. J. Biochem. 271 (2004) 3414–3420. [PMID: 15291818]
[EC 3.2.1.10 created 1961, modified 2000, modified 2013]
 
 
EC 3.2.1.41     
Accepted name: pullulanase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the α- and β-limit dextrins of amylopectin and glycogen
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Other name(s): limit dextrinase (erroneous); amylopectin 6-glucanohydrolase; bacterial debranching enzyme; debranching enzyme; α-dextrin endo-1,6-α-glucosidase; R-enzyme; pullulan α-1,6-glucanohydrolase
Systematic name: pullulan 6-α-glucanohydrolase
Comments: Different from EC 3.2.1.142 (limit dextrinase) in its action on glycogen, and its rate of hydrolysis of limit dextrins. Its action on amylopectin is complete. Maltose is the smallest sugar that it can release from an α-(1→6)-linkage.
References:
1.  Lee, E.Y.C. and Whelan, W.J. Glycogen and starch debranching enzymes. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 5, Academic Press, New York, 1972, pp. 191–234.
2.  Bender, H. and Wallenfels, K. Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes. Methods Enzymol. 8 (1966) 555–559.
3.  Manners, D.J. Observations on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci. 44 (1997) 83–85.
[EC 3.2.1.41 created 1972, modified 1976, modified 2000 (EC 3.2.1.69 created 1972, incorporated 1976)]
 
 
EC 3.2.1.57     
Accepted name: isopullulanase
Reaction: Hydrolysis of pullulan to isopanose (6-α-maltosylglucose)
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Systematic name: pullulan 4-glucanohydrolase (isopanose-forming)
Comments: The enzyme has practically no action on starch. Panose (4-α-isomaltosylglucose) is hydrolysed to isomaltose and glucose. cf. EC 3.2.1.41 (pullulanase) and EC 3.2.1.135 (neopullulanase).
References:
1.  Sakano, Y., Masuda, N. and Kobayashi, T. Hydrolysis of pullulan by a novel enzyme from Aspergillus niger. Agric. Biol. Chem. 35 (1971) 971–973.
[EC 3.2.1.57 created 1972]
 
 
EC 3.2.1.68     
Accepted name: isoamylase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Other name(s): debranching enzyme; glycogen α-1,6-glucanohydrolase
Systematic name: glycogen 6-α-D-glucanohydrolase
Comments: Also readily hydrolyses amylopectin. Differs from EC 3.2.1.41 (pullulanase) and EC 3.2.1.142 (limit dextrinase) by its inability to hydrolyse pullulan, and by limited action on α-limit dextrins. Maltose is the smallest sugar it can release from an α-(1→6)-linkage.
References:
1.  Yokobayashi, K., Misaki, A. and Harada, T. Purification and properties of Pseudomonas isoamylase. Biochim. Biophys. Acta 212 (1970) 458–469. [PMID: 5456995]
[EC 3.2.1.68 created 1972, modified 1976, modified 2000]
 
 
EC 3.2.1.69      
Deleted entry:  amylopectin 6-glucanohydrolase. Now included with EC 3.2.1.41 pullulanase
[EC 3.2.1.69 created 1972, deleted 1976]
 
 
EC 3.2.1.135     
Accepted name: neopullulanase
Reaction: Hydrolysis of pullulan to panose (6-α-D-glucosylmaltose)
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Other name(s): pullulanase II
Systematic name: pullulan 4-D-glucanohydrolase (panose-forming)
Comments: cf. EC 3.2.1.41 (pullulanase ) and EC 3.2.1.57 (isopullulanase).
References:
1.  Imanaka, T. and Kuriki, T. Pattern of action of Bacillus stearothermophilus neopullulanase on pullulan. J. Bacteriol. 171 (1989) 369–374. [PMID: 2914851]
[EC 3.2.1.135 created 1992]
 
 
EC 3.2.1.142     
Accepted name: limit dextrinase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in α- and β-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Other name(s): R-enzyme; amylopectin-1,6-glucosidase; dextrin α-1,6-glucanohydrolase
Systematic name: dextrin 6-α-glucanohydrolase
Comments: Plant enzymes with little or no action on glycogen. Action on amylopectin is incomplete, but action on α-limit dextrins is complete. Maltose is the smallest sugar it can release from an α-(1→6)-linkage.
References:
1.  Gordon, R.W., Manners, D.J. and Stark, J.R. The limit dextrinase of the broad bean (Vicia faba). Carbohydr. Res. 42 (1975) 125–134.
2.  Manners, D.J. Observations on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci. 44 (1997) 83–85.
[EC 3.2.1.142 created 2000]
 
 
EC 4.2.1.90     
Accepted name: L-rhamnonate dehydratase
Reaction: L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
Other name(s): L-rhamnonate hydro-lyase
Systematic name: L-rhamnonate hydro-lyase (2-dehydro-3-deoxy-L-rhamnonate-forming)
References:
1.  Rigo, L.U., Maréchal, L.R., Vieira, M.M. and Veiga, L.A. Oxidative pathway for L-rhamnose degradation in Pallularia pullulans. Can. J. Microbiol. 31 (1985) 817–822.
[EC 4.2.1.90 created 1989]