3.2.1.81: beta-agarase
This is an abbreviated version!
For detailed information about beta-agarase, go to the full flat file.
Word Map on EC 3.2.1.81
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3.2.1.81
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neoagarotetraose
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neoagarobiose
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agarolytic
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neoagarohexaose
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agar-degrading
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pseudoalteromonas
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agarivorans
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atlantica
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microbulbifer
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neoagaro-oligosaccharides
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galactanivorans
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gracilaria
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zobellia
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alteromonas
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catenovulum
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porphyran
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degradans
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saccharophagus
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flammeovirga
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carrageenase
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exo-type
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tat-dependent
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industry
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synthesis
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analysis
- 3.2.1.81
- neoagarotetraose
- neoagarobiose
- agarolytic
- neoagarohexaose
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agar-degrading
- pseudoalteromonas
- agarivorans
- atlantica
- microbulbifer
- neoagaro-oligosaccharides
- galactanivorans
- gracilaria
- zobellia
- alteromonas
- catenovulum
- porphyran
- degradans
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saccharophagus
- flammeovirga
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carrageenase
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exo-type
-
tat-dependent
- industry
- synthesis
- analysis
Reaction
Synonyms
AGA, Aga21, Aga50D, AgaA, AgaAc, AgaB, AgaB34, AgaC, AgaD, AgaP, agarase, Agarase 0107, agarase AG-a, AgaYT, beta-agarase, beta-agarase A, beta-agarase B, beta-agarase C, beta-agarase D, beta-agarase-a, DagA, endo-type beta-agarase, LSL-1, N3-1 protein, PjaA, RagaA11, YM01-1
ECTree
3.2.1.81 beta-agaraseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.81 - beta-agarase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L122Q
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shows similar thermostability with wild-type AgaB, raises specific activity 1.3fold
L122Q/N446I
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has higher thermostability and slightly increased specific activity (1.1fold) than wild-type AgaB. Melting temperature of S2 is 4.6°C higher than that of wild-type AgaB, and the half-life of S2 is 350 min at 40°C, which is 18.4fold longer than that of the wild-type enzyme. Comparable pH stability and optimum pH and temperature profiles as the wild-type
N103T
the mutant shows specific activity similar to the wild type enzyme
N446I
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has similar enhanced thermostability as mutant L122Q/N446I, and decreased specific activity by 10-20% as compared to the wild-type
N446L
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the half-life at 40°C is 12.9fold longer than that of wild-type AgaB
N446V
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the half-life at 40°C is 18.2fold longer than that of wild-type AgaB
S182I
the mutant shows specific activity similar to the wild type enzyme
V109G/V110C/T111H/S112L
the mutant shows severely reduced specific activity
E99K
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the mutant shows 140% relative activity compared to the wild type enzyme
E99K/T307I
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the mutant shows 200% relative activity compared to the wild type enzyme
T307I
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the mutant shows 190% relative activity compared to the wild type enzyme
E99K
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the mutant shows 140% relative activity compared to the wild type enzyme
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E99K/T307I
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the mutant shows 200% relative activity compared to the wild type enzyme
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T307I
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the mutant shows 190% relative activity compared to the wild type enzyme
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additional information
additional information
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construction of two C-terminally truncated forms of enzyme lacking 127 and 182 amino acids, the protein lacking 127 amino acids has a lower Km than wild type and higher thermal stability at 50°C
additional information
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construction of two C-terminally truncated forms of enzyme lacking 127 and 182 amino acids, the protein lacking 127 amino acids has a lower Km than wild type and higher thermal stability at 50°C
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additional information
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expression in Escherichia coli of full-length protein, of the catalytic module, and of the carbohydrate binding module. The catalytic module alone exhibits 50fold higher acivity than the full-length enzyme
additional information
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inactive mutant A-E147S, crystallization data
