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Literature summary for 2.4.1.19 extracted from

  • Nakagawa, Y.; Takada, M.; Ogawa, K.; Hatada, Y.; Horikoshi, K.
    Site-directed mutations in alanine 223 and glycine 255 in the acceptor site of gamma-cyclodextrin glucanotransferase from alkalophilic Bacillus clarkii 7364 affect cyclodextrin production (2006), J. Biochem., 140, 329-336.
    View publication on PubMed
Search for more literature for 2.4.1.19

Protein Variants

Protein Variants Comment Organism
A223H mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase Evansella clarkii
A223K mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase Evansella clarkii
A223R mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5 Evansella clarkii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
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 Evansella clarkii

Organism

Organism UniProt Comment Textmining
Evansella clarkii
-
-
-
Evansella clarkii 7364
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch
-
 Evansella clarkii gamma-cyclodextrin
-
 ?
starch
-
 Evansella clarkii 7364 gamma-cyclodextrin
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
 around, wild-type enzyme and mutant enzymes A223H, A223R and A223K, gamma-cyclodextrin-forming activity Evansella clarkii