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Literature summary for 2.4.1.25 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
Search for more literature for 2.4.1.25

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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]

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

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q8NNA7
-
-
Corynebacterium glutamicum DSM 20300 Q8NNA7
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap affinity column chromatography Corynebacterium glutamicum

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
amylomaltase
-
 Corynebacterium glutamicum

Turnover Number [1/s]

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

kcat/KM [mM/s]

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