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Literature summary extracted from

  • Nakajima, M.; Fushinobu, S.; Imamura, H.; Shoun, H.; Wakagi, T.
    Crystallization and preliminary X-ray analysis of cytosolic alpha-mannosidase from Thermotoga maritima (2006), Acta Crystallogr. Sect. F, 62, 104-105.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.24 TM1851, expression in Escherichia coli Thermotoga maritima
3.2.1.114 TM1851, expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.24 purified recombinant TM1851, sitting drop vapour diffusion method, optimal conditions: 0.001 ml of protein solution containing 5.3 mg/ml protein in 5 mM sodium phosphate and 150 mM NaCl, pH 6.8, mixed with an equal volume of reservoir solution containing 4% w/v PEG 6000, 50 mM sodium phosphate, pH 6.0, and 0.5 M NaCl, 1 day at 25°C, X-ray diffraction structure determination and preliminary analysis at 2.9 A resolution Thermotoga maritima
3.2.1.114 purified recombinant TM1851, sitting drop vapour diffusion method, optimal conditions: 0.001 ml of protein solution containing 5.3 mg/ml protein in 5 mM sodium phosphate and 150 mM NaCl, pH 6.8, mixed with an equal volume of reservoir solution containing 4% w/v PEG 6000, 50 mM sodium phosphate, pH 6.0, and 0.5 M NaCl, 1 day at 25°C, X-ray diffraction structure determination and preliminary analysis at 2.9 A resolution Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.24 cytosol
-
 Thermotoga maritima 5829
-
3.2.1.114 cytosol
-
 Thermotoga maritima 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.24 Cd2+ preferred divalent cation Thermotoga maritima
3.2.1.24 Co2+ preferred divalent cation Thermotoga maritima
3.2.1.114 Cd2+ preferred divalent cation Thermotoga maritima
3.2.1.114 Co2+ preferred divalent cation Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.24 additional information Thermotoga maritima the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues ?
-
 ?
3.2.1.114 additional information Thermotoga maritima the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.24 Thermotoga maritima
-
-
-
3.2.1.114 Thermotoga maritima
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.24 recombinant TM1851 from Escherichia coli by ion exchange and hydroxyapatite chromatography, and gel filtration Thermotoga maritima
3.2.1.114 recombinant TM1851 from Escherichia coli by ion exchange and hydroxyapatite chromatography, and gel filtration Thermotoga maritima

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.24 4.2
-
 purified recombinant TM1851 Thermotoga maritima
3.2.1.114 4.2
-
 purified recombinant TM1851 Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.24 additional information the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues Thermotoga maritima ?
-
 ?
3.2.1.114 additional information the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues Thermotoga maritima ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.24 class II alpha-mannosidase
-
 Thermotoga maritima
3.2.1.24 More the enzyme belongs to the glycoside hydrolase family 38 Thermotoga maritima
3.2.1.24 TM1851
-
 Thermotoga maritima
3.2.1.114 class II alpha-mannosidase
-
 Thermotoga maritima
3.2.1.114 More the enzyme belongs to the glycoside hydrolase family 38 Thermotoga maritima
3.2.1.114 TM1851
-
 Thermotoga maritima