The enzyme catalyzes the hydrolysis of cerebroside 3-sulfate producing cerebroside and sulfate. It uses a divalent cation to perform the catalytic mechanism (PMID11124905).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 44 x | MG | magnesium | divalent cation | mononuclear | Coordinates substrate Increases electrophilicity Electrostatic stabiliser |
*It refers to the MACiE reference pdb: 1auk
| Metal/s Properties in Resting State | ||||||
| MG 44 x | Resting state enzyme (1e1z) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -von Bülow R, Schmidt B, Dierks T, von Figura K, Usón I Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. J Mol Biol. 2001 Jan 12;305(2):269-77.(MEDLINE:11124905) |
| - Some information have been also deduced from the MACiE mechanism model |