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EC 3.1.6.15 Details

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EC number

3.1.6.15

Accepted name

N-sulfoglucosamine-3-sulfatase

Reaction

Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin

Other name(s)

chondroitinsulfatase

Systematic name

N-sulfo-3-sulfoglucosamine 3-sulfohydrolase

Comment

The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue.

History

created 1984, modified 1989

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.1.1 Carboxylic-ester hydrolases

3.1.2 Thioester hydrolases

3.1.3 Phosphoric-monoester hydrolases

3.1.4 Phosphoric-diester hydrolases

3.1.5 Triphosphoric-monoester hydrolases

3.1.6 Sulfuric-ester hydrolases

3.1.7 Diphosphoric-monoester hydrolases

3.1.8 Phosphoric-triester hydrolases

3.1.11 Exodeoxyribonucleases producing 5′-phosphomonoesters

3.1.12 Exodeoxyribonucleases producing 3′-phosphomonoesters

3.1.13 Exoribonucleases producing 5′-phosphomonoesters

3.1.13.1 exoribonuclease II

3.1.13.2 exoribonuclease H

3.1.13.3 oligonucleotidase

3.1.13.4 poly(A)-specific ribonuclease

3.1.13.5 ribonuclease D

3.1.14 Exoribonucleases producing 3'-phosphomonoesters

3.1.15 Exonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters

3.1.16 Exonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters

3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters

3.1.22 Endodeoxyribonucleases producing 3'-phosphomonoesters

3.1.23 Site-specific endodeoxyribonucleases: cleavage is sequence specific (deleted sub-subclass)

3.1.24 Site specific endodeoxyribonucleases: cleavage is not sequence specific (deleted sub-subclass)

3.1.25 Site-specific endodeoxyribonucleases that are specific for altered bases

3.1.26 Endoribonucleases producing 5'-phosphomonoesters

3.1.27 Endoribonucleases producing 3'-phosphomonoesters

3.1.30 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters

3.1.31 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.10.1 Acting on sulfur-nitrogen bonds (only sub-subclass identified to date)

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)