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Literature summary extracted from

  • Tumhom, S.; Krusong, K.; Kidokoro, S.I.; Katoh, E.; Pongsawasdi, P.
    Significance of H461 at subsite +1 in substrate binding and transglucosylation activity of amylomaltase from Corynebacterium glutamicum (2018), Arch. Biochem. Biophys., 652, 3-8 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.25 expressed in Escherichia coli BL21(DE3) cells Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.25 H461A the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate Corynebacterium glutamicum
2.4.1.25 H461D the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate Corynebacterium glutamicum
2.4.1.25 H461R the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate Corynebacterium glutamicum
2.4.1.25 H461S the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate Corynebacterium glutamicum
2.4.1.25 H461W the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.25 16.9
-
 maltotriose wild type enzyme, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 35.1
-
 maltotriose mutant enzyme H461S, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 35.7
-
 maltotriose mutant enzyme H461A, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 36.2
-
 maltotriose mutant enzyme H461W, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 37.2
-
 maltotriose mutant enzyme H461D, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 37.4
-
 maltotriose mutant enzyme H461R, at pH 6.0 and 30°C Corynebacterium glutamicum

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Corynebacterium glutamicum Q8NNA7
-
-
2.4.1.25 Corynebacterium glutamicum DSM 20300 Q8NNA7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.25 HisTrap affinity column chromatography Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 maltotriose + glycosyl acceptor the wild type enzyme prefers maltotriose for disproportionation reaction Corynebacterium glutamicum maltose + D-glucose + maltooligosaccharides
-
 ?
2.4.1.25 maltotriose + glycosyl acceptor the wild type enzyme prefers maltotriose for disproportionation reaction Corynebacterium glutamicum DSM 20300 maltose + D-glucose + maltooligosaccharides
-
 ?
2.4.1.25 pea starch + glycosyl acceptor
-
 Corynebacterium glutamicum large-ring cyclodextrins
-
 ?
2.4.1.25 pea starch + glycosyl acceptor
-
 Corynebacterium glutamicum DSM 20300 large-ring cyclodextrins
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.25 ? x * 84000, SDS-PAGE Corynebacterium glutamicum

Synonyms

EC Number Synonyms Comment Organism
2.4.1.25 amylomaltase
-
 Corynebacterium glutamicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.25 120.8
-
 maltotriose mutant enzyme H461W, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 121.2
-
 maltotriose mutant enzyme H461A, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 122
-
 maltotriose mutant enzyme H461R, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 136
-
 maltotriose mutant enzyme H461S, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 143.7
-
 maltotriose mutant enzyme H461D, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 3033
-
 maltotriose wild type enzyme, at pH 6.0 and 30°C Corynebacterium glutamicum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.1.25 3.2
-
 maltotriose mutant enzyme H461R, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 3.3
-
 maltotriose mutant enzyme H461W, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 3.5
-
 maltotriose mutant enzyme H461A, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 3.7
-
 maltotriose mutant enzyme H461D, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 3.8
-
 maltotriose mutant enzyme H461S, at pH 6.0 and 30°C Corynebacterium glutamicum
2.4.1.25 180
-
 maltotriose wild type enzyme, at pH 6.0 and 30°C Corynebacterium glutamicum