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Literature summary for 3.2.1.1 extracted from

  • Siddiqui, K.S.; Poljak, A.; De Francisci, D.; Guerriero, G.; Pilak, O.; Burg, D.; Raftery, M.J.; Parkin, D.M.; Trewhella, J.; Cavicchioli, R.
    A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability (2010), Protein Eng. Des. Sel., 23, 769-780.
    View publication on PubMed
Search for more literature for 3.2.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
purified modified enzyme TAAMOD, vapour diffusion, 10 mg/ml protein in 10 mM Tris, pH 7.5, and 5 mM CaCl2 against a solution of 20% PEG 4000, 0.4 M ammonium sulfate and 0.1 M MES, pH 7.2, 2 weeks, X-ray diffraction structure determination and analysis at 2.4 A reolution Aspergillus oryzae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information activation thermodynamics for kinetic stability of native and modified enzymes, overview Aspergillus oryzae

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no requirement for Ca2+ Aspergillus oryzae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 the modified enzyme TAAMOD acquires a higher molecular weight than the native enzyme TAAUM by 2096 Da Aspergillus oryzae

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Aspergillus oryzae
-

Synonyms

Synonyms Comment Organism
TAA
-
 Aspergillus oryzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40 60 assay at Aspergillus oryzae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 at a temperature approximating the optimal temperature of 50°C, the modified enzyme TAAMOD has a 28fold higher t1/2-inact of 340 min compared with native enzyme TAAUM with 12 min Aspergillus oryzae
53
-
 t1/2 inact of the native enzyme TAAUM is 6 min, of the modified enzyme TAAMOD 140 min Aspergillus oryzae
55
-
 t1/2 inact of the native enzyme TAAUM is 4 min, of the modified enzyme TAAMOD 30 min Aspergillus oryzae
60
-
 t1/2 inact of the native enzyme TAAUM is 1 min, of the modified enzyme TAAMOD 6 min Aspergillus oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Aspergillus oryzae

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus oryzae the modified enzyme TAAMOD acquires a higher pI than the native enzyme TAAUM
-
 additional information

General Information

General Information Comment Organism
additional information enzyme modification using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride in the presence of a nucleophile, AME, to activate the carboxyl groups of the enzyme, comparisons in anion and cation exchange chromatographies and by native PAGE, overview. The modifications project into the bulk solvent. The enhanced thermostability leads to increased productivity Aspergillus oryzae