3.2.1.85: 6-phospho-beta-galactosidase

This is an abbreviated version!
For detailed information about 6-phospho-beta-galactosidase, go to the full flat file.

Reaction

Synonyms

6-phospho-beta-D-galactosidase, beta-D-phosphogalactosidase, beta-D-phosphogalactoside galactohydrolase, beta-Pgal, beta-phosphogalactosidase, BGase-III, Gan1D, LacG1, LacG2, P-beta-gal, P-beta-galactosidase, P-bgal, PBG, PGALase, phospho-beta-galactosidase

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.85 6-phospho-beta-galactosidase

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Results	in table
10	Activating Compound
1526	AA Sequence
1	Application
1	CAS Registry Number
17	Cloned(Commentary)
3	Crystallization (Commentary)
3	Expression
4	General Information
27	Inhibitors
2	kcat/KM [mM/s]
38	KM Value [mM]
3	Localization
18	Metals/Ions
18	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
48	Organism
5	Pathway
57	PDB ID
11	pH Optimum
3	pH Range
2	pH Stability
1	pI Value
13	Protein Variants
17	Purification (Commentary)
1	Reaction
1	Reaction Type
46	Reference
3	Source Tissue
13	Specific Activity [micromol/min/mg]
1	Storage Stability
79	Substrates and Products (Substrate)
6	Subunits
52	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
4	Temperature Stability [°C]
16	Turnover Number [1/s]

Engineering

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Engineering on EC 3.2.1.85 - 6-phospho-beta-galactosidase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

E170Q

Geobacillus stearothermophilus

W8QF82

catalytic mutant

750522

W433A

Geobacillus stearothermophilus

W8QF82

the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity

750522

W433M

Geobacillus stearothermophilus

W8QF82

the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity

750522

E170Q

Geobacillus stearothermophilus T-1

-

catalytic mutant

-

W433A

Geobacillus stearothermophilus T-1

-

the mutation shifts the enzyme specificity from dual activity to a significant preference toward 6-phospho-beta-glucosidase activity

-

K435V/Y437F

Lactococcus lactis

P11546

significantly reduced substrate binding and turnover

657216

S428D/K435V/Y437F

Lactococcus lactis

P11546

no activity

657216

W429A

Lactococcus lactis

P11546

improved specificity for glucosides

657216

E160Q

Staphylococcus aureus

-

1000fold reduction in activity compared to wild type

208852

E375Q

Staphylococcus aureus

-

complete loss of activity

208852

G332R

Staphylococcus aureus

-

complete loss of catalytic activity, but same behavior during purification and in affinity to antisera as wild type

208852

additional information

2 entries

additional information

Lactococcus lactis

-

construction of a disruption mutant of gene bglS, encoding phospho-beta-glucosidase, in phospho-beta-galactosidase-deficient strain IL1403, genetic organization and chromosomal localizations in mutant strain IL1403 showig the beta-galactosidase-negative phenotype

663711

additional information

Staphylococcus aureus

-

hybrid protein with protein A

208851