N-acetylgalactosamine-6-sulfatase

The enzyme N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4)^[1]^[2]^[3] catalyzes the chemical reaction of cleaving off the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of the macromolecule chondroitin sulfate and, similarly, of the D-galactose 6-sulfate units of the macromolecule keratan sulfate.

This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase. Other names in common use include chondroitin sulfatase, chondroitinase, galactose-6-sulfate sulfatase, acetylgalactosamine 6-sulfatase, N-acetylgalactosamine-6-sulfate sulfatase, and N-acetylgalactosamine 6-sulfatase. This enzyme participates in glycosaminoglycan degradation and degradation of glycan structures.

Deficiency

Morquio syndrome is a rare birth defect caused by a deficiency in this essential enzyme.^[4]^[5] Treatment options include enzyme replacement therapy with a synthetic version of the enzyme called elosulfase alfa.

References

^ Epstein EH, Leventhal ME (1981). "Steroid sulfatase of human leukocytes and epidermis and the diagnosis of recessive X-linked ichthyosis". J. Clin. Invest. 67 (5): 1257–62. doi:10.1172/JCI110153. PMC 370691. PMID 6939689.
^ Sorensen SH, Noren O, Sjostrom H, Danielsen EM (1982). "Amphiphilic pig intestinal microvillus maltase/glucoamylase Structure and specificity". Eur. J. Biochem. 126 (3): 559–68. doi:10.1111/j.1432-1033.1982.tb06817.x. PMID 6814909.
^ Lim CT, Horwitz AL (1981). "Purification and properties of human N-acetylgalactosamine-6-sulfate sulfatase". Biochim. Biophys. Acta. 657 (2): 344–55. doi:10.1016/0005-2744(81)90320-x. PMID 7213753.
^ Glossl J, Kresse H (1982). "Impaired degradation of keratan sulphate by Morquio A fibroblasts". Biochem. J. 203 (1): 335–8. PMC 1158229. PMID 6213226.
^ Yutaka T, Okada S, Kato T, Inui K, Yabuuhi H (1982). "Galactose 6-sulfate sulfatase activity in Morquio syndrome". Clin. Chim. Acta. 122 (2): 169–80. doi:10.1016/0009-8981(82)90276-5. PMID 6809361.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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