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2.4.1.25: 4-alpha-glucanotransferase

This is an abbreviated version!
For detailed information about 4-alpha-glucanotransferase, go to the full flat file.

Word Map on EC 2.4.1.25

Reaction

maltononaose
+
maltotriose
=
maltoundecaose
 +
D-glucose

Synonyms

(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-glycosyltransferase, 4-alpha-D-alpha-glucanotransferase, 4-alpha-glucanotransferase, 4-alpha-GTase, 4alphaGT, 4alphaGTase, AgtA, AgtB, alpha-1,4-glucanotransferase, alpha-1,4-transferase, alpha-amylase-like transglycosylase, alpha-glucanotransferase, alphaGT, alphaGTase, AMase, amylmaltase, amylomaltase, At2g40840, CGTase, Cqm1, D-enzyme, debranching enzyme, debranching enzyme maltodextrin glycosyltransferase, dextrin glycosyltransferase, dextrin glycosyltransferase,, dextrin transglycosylase, disproportionating enzyme, DPE1, DPE2, EC 2.4.1.3, exo-MGTase, GDE, GH77, GH77 amylomaltase, glycogen debranching enzyme, GTase, MalQ, maltodextrin glycosyltransferase, maltosyltransferase, MgtA, MmtA, More, MQ-01, MTase, oligo-1,4-1,4-glucantransferase, PyAMase, TAalphaGT, TAalphaGTase, TLGT, TmalphaGT, TreX, TS alpha GTase, TSalphaGT

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.25 4-alpha-glucanotransferase

Engineering

Engineering on EC 2.4.1.25 - 4-alpha-glucanotransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
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
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
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
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
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
N287Y
-
the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose
Y172A
-
mutant exhibits lower disproportionation, cyclization, and hydrolysis activities than the wild-type. The kcat/Km of the disproportionation reaction for the Y172A enzyme is 2.8fold lower than that of wild-type. The Y172A enzyme shows a product pattern different from that of wild-type at a long incubation time. The principal large-ring cyclodextrin products of the Y172A mutant are a cycloamylose mixture with a degree of polymerization of 28 or 29
Y418A
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418D
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418F
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 29-33 from pea starch
Y418R
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418S
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418W
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
-
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
-
N287Y
-
the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose
-
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
-
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
-
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
-
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
-
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
-
W229H
-
kcat/KM value of transglycosylation activity significantly decreases to about 15% of wild-type, kcat/Km value of hydrolysis activity changes little
D214N
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
E123Q
-
the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme
E129Q
-
the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme
D214N
-
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
-
F251G
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity
Q256G
mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose
W258G
mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities
D293A
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D293N
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D294S
site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme
D395A
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D395N
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340A
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340Q
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E758Q
the mutant shows highly reduced activity compared to the wild-type enzyme
F366L
site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme
D293A
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
D293N
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
D395N
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
E340A
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
E340Q
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
additional information