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 .

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2026.1 (March 2026)