Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Myrosinase MA1  

UniProtKB / Swiss-Prot ID :  MYRA_SINAL

Gene Name (Synonyms) :  -
 

Species :  Sinapis alba (White mustard) (Brassica hirta). 

Subcellular Localization :  Vacuole. 

Protein Function :  Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. 

Protein Sequence DEEITCQENLPFTCGNTDALNSSSFSSDFIFGVASSAYQIEGTIGRGLNIWDGFTHRYPNKSGPDHGNGD...
Predicted Secondary Structure CCCEEECCCCCCCCCCHHHHCCCCCCCCCEEEEEEEEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
21N-linked (GlcNAc...).TDALNSSSF
HHHHCCCCC
41.38UniProtKB
Link
60N-linked (GlcNAc...).HRYPNKSGP
CCCCCCCCC
42.04UniProtKB
Link
90N-linked (GlcNAc...).LDELNATGY
HHHHCCCEE
33.15UniProtKB
Link
218N-linked (GlcNAc...).CYAGNSSTE
CCCCCCHHH
25.31UniProtKB
Link
244N-linked (GlcNAc...).LYRKNYTHQ
HHHHCCCCC
37.63UniProtKB
Link
265N-linked (GlcNAc...).FLPYNDTDR
CCCCCCCCH
43.71UniProtKB
Link
292N-linked (GlcNAc...).GPLTNGTYP
HHHCCCCCH
48.79UniProtKB
Link
343N-linked (GlcNAc...).PNPVNSTNH
CCCCCCCCC
44.36UniProtKB
Link
346N-linked (GlcNAc...).VNSTNHTAM
CCCCCCCCC
30.27UniProtKB
Link
361N-linked (GlcNAc...).LTYINASGH
CCCCCCCCC
20.03UniProtKB
Link
482N-linked (GlcNAc...).IDWNNVTDR
EECCCCCCC
33.54UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The crystal structures of Sinapis alba myrosinase and a covalentglycosyl-enzyme intermediate provide insights into the substraterecognition and active-site machinery of an S-glycosidase.";
Burmeister W.P., Cottaz S., Driguez H., Iori R., Palmieri S.,Henrissat B.;
Structure 5:663-675(1997).
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), SUBUNIT, AND GLYCOSYLATION ATASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343;ASN-346; ASN-361 AND ASN-482.
"High resolution X-ray crystallography shows that ascorbate is acofactor for myrosinase and substitutes for the function of thecatalytic base.";
Burmeister W.P., Cottaz S., Rollin P., Vasella A., Henrissat B.;
J. Biol. Chem. 275:39385-39393(2000).
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ASCORBATE ANDTRANSITION STATE ANALOGS, SUBUNIT, AND GLYCOSYLATION AT ASN-21;ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343; ASN-346;ASN-361 AND ASN-482.
"The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors.";
Bourderioux A., Lefoix M., Gueyrard D., Tatibouet A., Cottaz S.,Arzt S., Burmeister W.P., Rollin P.;
Org. Biomol. Chem. 3:1872-1879(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, AND GLYCOSYLATION ATASN-21; ASN-60; ASN-90; ASN-218; ASN-244; ASN-265; ASN-292; ASN-343;ASN-346; ASN-361 AND ASN-482.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures