3.2.1.B1: extracellular agarase

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For detailed information about extracellular agarase, go to the full flat file.

Reaction

hydrolysis of 1,3-beta-D-galactosidic linkages in agarose, giving the octamer as the predominant product =

Synonyms

Aga21, AgaA, AgaA7, AgaB, AgaB1, AgaC, AgaG1, agaM1, agarase AG-b, agarase-a, agarase-b, beta-agarase, beta-agarase AgaB, endo-acting beta-agarase, endo-type beta-agarase, exo-beta-agarase, extracellular beta-agarase, NifU, YM01-3

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.B1 extracellular agarase

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Results	in table
11	Activating Compound
7	AA Sequence
1	Application
12	Cloned(Commentary)
3	Expression
3	General Stability
1	IC50 Value
167	Inhibitors
1	kcat/KM [mM/s]
4	KM Value [mM]
40	Localization
47	Metals/Ions
24	Molecular Weight [Da]
29	Natural Substrates/ Products (Substrates)
50	Organism
27	pH Optimum
17	pH Range
17	pH Stability
4	pI Value
1	Posttranslational Modification
5	Protein Variants
22	Purification (Commentary)
2	Reaction
48	Reference
1	Renatured (Commentary)
10	Source Tissue
15	Specific Activity [micromol/min/mg]
1	Storage Stability
88	Substrates and Products (Substrate)
47	Subunits
49	Synonyms
1	Systematic Name
29	Temperature Optimum [°C]
19	Temperature Range [°C]
27	Temperature Stability [°C]
6	Turnover Number [1/s]

Engineering

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Engineering on EC 3.2.1.B1 - extracellular agarase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

L122Q

Pseudoalteromonas sp.

-

mutant enzyme shows similar thermostability with wild-type AgaB. Specific activity 1.3fold higher than that of wild-type enzyme

695671

N446I

Pseudoalteromonas sp.

-

mutant enzyme has enhanced thermostability. 10-20% decrease of the specific activity compared to wild-type enzyme

695671

N446L

Pseudoalteromonas sp.

-

half-life of mutant enzyme at 40°C is 12.9fold longer than that of wild-type AgaB

695671

N446V

Pseudoalteromonas sp.

-

half-life of mutant enzyme at 40°C is 18.2fold longer than that of wild-type AgaB

695671

additional information

Pseudoalteromonas sp.

-

to increase the thermostability of beta-agarase AgaB by directed evolution, the mutant gene libraries are generated by error-prone polymerase chain reaction and deoxyribonucleic acid shuffling. A mutant S2 is obtained through two rounds of error-prone polymerase chain reaction and a single round of DNA shuffling and selection. It has higher thermostability and slightly increased catalytic activity than wild-type AgaB. Melting temperature (Tm) of S2, as determined by circular dichroism, 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 18.4-fold longer than that of the wild-type enzyme. Saturation mutagenesis and hydrophobic cluster analysis indicate that hydrophobic interaction might be the key factor that enhances the enzyme stability

695671