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Literature summary for 3.2.1.78 extracted from

  • Kim, M.K.; An, Y.J.; Song, J.M.; Jeong, C.S.; Kang, M.H.; Kwon, K.K.; Lee, Y.H.; Cha, S.S.
    Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus (2014), Proteins, 82, 3217-3223.
    View publication on PubMed
Search for more literature for 3.2.1.78

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in apoform and in complex with mannopentaose, the precipitant solution contains 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis, modelling Cryptopygus antarcticus

Organism

Organism UniProt Comment Textmining
Cryptopygus antarcticus B4XC07
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mannopentaose + H2O
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 Cryptopygus antarcticus mannose + mannotetraose
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 ?

Subunits

Subunits Comment Organism
More the enzyme adopts a TIM (beta/alpha)8-barrel fold Cryptopygus antarcticus

Synonyms

Synonyms Comment Organism
beta-1,4-D-mannanase
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 Cryptopygus antarcticus
CaMan
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 Cryptopygus antarcticus
cold-adapted beta-mannanase
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 Cryptopygus antarcticus
endo-beta-1,4-D-mannanase
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 Cryptopygus antarcticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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 cold-adapted beta-mannanase Cryptopygus antarcticus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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 60 the enzyme shows 20-40% of its maximum activity at 0-4°C and has its optimum at 30°C, about 10% of maximal activity at 50-60°C, inactivation at 70°C, profile overview Cryptopygus antarcticus

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5 Cryptopygus antarcticus
additional information the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview Cryptopygus antarcticus