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Literature summary extracted from

  • Fujii, K.; Minagawa, H.; Terada, Y.; Takaha, T.; Kuriki, T.; Shimada, J.; Kaneko, H.
    Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase (2007), J. Biosci. Bioeng., 103, 167-173.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.25 additional information the amino acid substitution at Y54 or Y101 for removing their aromatic side chain increases cyclization activity, intra-molecular transglycosylation reaction, but decreases disproportionation, coupling and hydrolytic activities, inter-molecular reactions Thermus aquaticus
2.4.1.25 Y54A site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54C site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54D site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54E site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54F site-directed mutagenesis, the mutant shows increased coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54G site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54H site-directed mutagenesis, the mutant shows increased coupling and reduced disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54I site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54K site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54L site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54M site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54N site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54P site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54Q site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54R site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54S site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54T site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54V site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus
2.4.1.25 Y54W site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme Thermus aquaticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.25 additional information Thermus aquaticus amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Thermus aquaticus B7A9X4
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.25 additional information
-
 disproportionation and coupling activities of wild-type and Y54 mutated enzymes, overview Thermus aquaticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 (alpha-1,4 glucan)m + (alpha-1,4 glucan)n
-
 Thermus aquaticus (alpha-1,4 glucan)m-x + (alpha-1,4 glucan)n+x
-
 r
2.4.1.25 additional information amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan Thermus aquaticus ?
-
 ?
2.4.1.25 additional information the enzyme contains two substrate binding sites involving residues Y54 or Y101, structure and localization, overview. The binding of glucan substrate to the second glucan binding site through an interaction with the aromatic side chains of Y54 and Y101 is a trigger for the enzyme to take a completely active conformation for all four types of activity, but prevents the cyclization reaction to occur since the flexibility of the glucan is restricted by such binding. Synthesis of cycloamylose, overview Thermus aquaticus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.25 amylomaltase
-
 Thermus aquaticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.25 70
-
 assay at Thermus aquaticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.25 5.5
-
 assay at Thermus aquaticus