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=='''Several functions:'''==
The predicted function based on the evolution and structure


[http://amigo.geneontology.org/cgi-bin/amigo/go.cgi?view=details&depth=1&query=0016787 1. Hydrolase Activity]
<font size = "4">'''Hydrolase'''</font>


[http://amigo.geneontology.org/cgi-bin/amigo/go.cgi?view=details&depth=1&query=0000287 2. Magnesium Ion Binding]


[http://amigo.geneontology.org/cgi-bin/amigo/go.cgi?view=details&depth=1&query=0050124 3. N-acylneuraminate-9-phosphatase Activity]
[[Image:Document18_01.png]]


[http://amigo.geneontology.org/cgi-bin/amigo/go.cgi?view=details&depth=1&query=0008967 4. Phosphoglycolate Phosphatase Activity]
Hydrolyase catalyze the hydrosis of the chemical bond between A and B, resulting of 2 simple molecules
 
 
* Hydrolase
** Catalyze hydrolysis reaction 
** Addition of the hydrogen and hydroxyl ions of water
** Splitting into 2 or more simpler molecules
** EC class 3
 
 
 
== Function of sulfatases ==
 
Sulfatases are enzymes,which hydrolyse sulfate ester bonds of substrates.
Most of the family members has shown to contain a highly conserved cystine residue and a bivalent metal binding site.
 
 
 
 
 
== Functional site==
MSA data revealed some conserved residues on the sequence. They were mapped on the three dimantional structure.
 
[[Image:Zn_Cl_surface]]
 
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Click here to go [http://compbio.chemistry.uq.edu.au/mediawiki/index.php/BIOL3004_2007 ''Back'']

Latest revision as of 09:44, 20 May 2008

The predicted function based on the evolution and structure

Hydrolase


Document18 01.png

Hydrolyase catalyze the hydrosis of the chemical bond between A and B, resulting of 2 simple molecules


  • Hydrolase
    • Catalyze hydrolysis reaction
    • Addition of the hydrogen and hydroxyl ions of water
    • Splitting into 2 or more simpler molecules
    • EC class 3


Function of sulfatases

Sulfatases are enzymes,which hydrolyse sulfate ester bonds of substrates. Most of the family members has shown to contain a highly conserved cystine residue and a bivalent metal binding site.



Functional site

MSA data revealed some conserved residues on the sequence. They were mapped on the three dimantional structure.

File:Zn Cl surface


Click here to go Back