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4.2.2.7: heparin lyase

This is an abbreviated version!
For detailed information about heparin lyase, go to the full flat file.

Word Map on EC 4.2.2.7

Reaction

Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends =

Synonyms

Hep III, HepA, heparin degrading enzyme, Heparin eliminase, heparin lyase, heparin lyase 1, heparin lyase I, heparin lyase II, Heparinase, heparinase I, heparinase II, heparitinase II, heparitinase III, HepI, HepII, HepP, HMPREF1016_02668, Lyase, heparin, PA14_23430, Pedsa_1818, PL12a

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.7 heparin lyase

Engineering

Engineering on EC 4.2.2.7 - heparin lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA 156-221
-
no activity
DELTA 191-213
-
about 5% of wild-type activity
H151A
-
no activity
K185A
-
about 100% of wild-type activity
K252A
-
about 40% of wild-type activity
K353A
-
no activity
Q149A
-
no activity
Q223A
-
about 40% of wild-type activity
Q22A
-
about 20% of wild-type activity
R156A
-
about 90% of wild-type activity
Y357A
-
no activity
H151A
-
no activity
-
K185A
-
about 100% of wild-type activity
-
K353A
-
no activity
-
Q22A
-
about 20% of wild-type activity
-
R156A
-
about 90% of wild-type activity
-
D210A
-
mutation does not affect the product profile compared to the wild type anzyme
D212A
-
mutation does not affect the product profile compared to the wild type anzyme
E207A
-
mutation does not affect the product profile compared to the wild type anzyme
E381A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
G213A
-
mutation does not affect the product profile compared to the wild type anzyme
G378A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
H202/H406A
-
His-tagged version expressed in Escherichia coli BL21(DE3)
H202A
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
H202A/Y257A
-
His-tagged version expressed in Escherichia coli BL21(DE3)
H406A
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
I133T/P316T
mutant displays about 7fold increase in catalytic efficiency
N375A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
N405A
-
site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows broadened substrate specificity and cleaves the resistant linkage proximate to the 3-O-sulfoglucosamine residue
N405A/H406A
-
site-directed mutagenesis
N405G
-
site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows broadened substrate specificity and cleaves the resistant linkage proximate to the 3-O-sulfoglucosamine residue
N405G/H406A
-
site-directed mutagenesis
S377A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
T216A
-
mutation does not affect the product profile compared to the wild type anzyme
T373A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
T382A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
Y257A
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
Y257A/H406A
-
His-tagged version expressed in Escherichia coli BL21(DE3)
Y257F
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
Y379A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
additional information
-
construction of several double and triple mutants of the calcium-coordinating residues