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Literature summary for 4.2.2.8 extracted from

  • Hu, G.; Shao, M.; Gao, X.; Wang, F.; Liu, C.
    Probing cleavage promiscuity of heparinase III towards chemoenzymatically synthetic heparan sulfate oligosaccharides (2017), Carbohydr. Polym., 173, 276-285 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pedobacter heparinus

Organism

Organism UniProt Comment Textmining
Pedobacter heparinus
-
-
-
Pedobacter heparinus Q05819
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcN-(1->4)-beta-D-GlcA
-
Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcN
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc-(1->4)-beta-D-GlcA
-
Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc-(1->4)-beta-D-GlcA about 15fold higher catalytic efficiency than with 4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc6S-(1->4)-beta-D-GlcA
-
Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc6S
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA
-
Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNS
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS6S-(1->4)-beta-D-GlcA
-
Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNS6S
-
?
4-nitrophenyl beta-D-GlcA-(1->4>)-alpha-D-GlcNS-(1->4)-beta-IdoA2S-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA
-
Pedobacter heparinus 4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4>)-alpha-D-GlcNS-(1->4)-beta-IdoA2S-(1->4)-alpha-D-GlcNS
-
?
IdoA2S-containing sulfated heparan hexasaccharide
-
Pedobacter heparinus ?
-
?
IdoA2S-containing sulfated heparan pentasaccharide
-
Pedobacter heparinus ?
-
?
additional information the enzyme is capable of tolerating heparin sulfate trimers containing single GlcNH2, GlcNAc6S or GlcNS6S residues, but is more than 20 times less reactive towards the secondary cleavage sites compared with the counterpart primary substrates. Hep III hydrolyzes the iduronic acid containing glyosidic linkage (GlcNS-IdoA) at similar catalytic efficiency to GlcNS-GlcA, but has a slight preference toward GlcNS-GlcA linkage over GlcNS-IdoA at the beginning of catalytic reaction Pedobacter heparinus ?
-
?
additional information the susceptibility of the oligosaccharide substrates to the enzymatic digestion is size-dependent. Hep III has a preference for cleavage of the internal glycosidic linkages over those near to nonreducing/reducing ends . Hep III hydrolyzes the IdoA-containing glyosidic linkage (GlcNS-IdoA) at similar catalytic efficiency to GlcNS-GlcA, but has a slight preference toward GlcNS-GlcA linkage over GlcNS-IdoA at the beginning of catalytic reaction. The IdoA2S residue significantly decreases the reactivity of Hep III towards its adjacent GlcNS-GlcA at reducing end of heparan sulfate oligosaccharides, but shows no obvious influence on its nearby cleavage site at the nonreducing end Pedobacter heparinus ?
-
?
N-sulfated heparan pentasaccharide
-
Pedobacter heparinus ?
-
?