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Information on EC 2.8.2.30 - [heparan sulfate]-glucosamine 3-sulfotransferase 3 and Organism(s) Mus musculus and UniProt Accession Q9QZS6

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EC Tree
IUBMB Comments
Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN*-> and -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN6S*-> (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells . There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes . The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].
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Mus musculus
UNIPROT: Q9QZS6
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
hs3st3b1, isoform 3a, hs6st3, 3-ost-3, 3-ost-3a, hs3st3a1, hs3st3b, 3-ost3a, heparan sulfate 3-o-sulfotransferase, hs3st, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-OST-3
-
-
3-OST-3A
-
-
-
-
3-OST-3B
-
-
-
-
glucosaminyl 3-O-sulfotransferase 3a,3b
-
-
-
-
heparan sulfate 3-O-sulfotransferase 3
-
-
heparan sulfate D-glucosamine 3-O-sulfotransferase 3A
-
-
-
-
HS3ST3A
-
-
-
-
HS3ST3B
-
-
-
-
isoenzyme 3a
-
-
-
-
isoenzyme 3b
-
-
-
-
isoform 3a
-
-
-
-
isoform 3b
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN*-> and -> undetermined 2-sulfo-uronic acid-> GlcN2S-> IdoA2S-> GlcN6S*-> (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes [3]. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].
CAS REGISTRY NUMBER
COMMENTARY hide
183257-54-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
show the reaction diagram
3-O-sulfonation of heparan sulfate by isoenzyme 3A and 3B generates binding sites for the HSV-1 glycoprotein gD and initiation of virus entry
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
show the reaction diagram
3-O-sulfonation of heparan sulfate by isoenzyme 3A and 3B generates binding sites for the HSV-1 glycoprotein gD and initiation of virus entry
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HS3SB_MOUSE
390
1
43296
Swiss-Prot
Mitochondrion (Reliability: 4)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K259A
-
the mutant shows 13.1% activity compared to the wild type enzyme
T256A
-
the mutant shows 101.5% activity compared to the wild type enzyme
T256E
-
the mutant shows 13.1% activity compared to the wild type enzyme
T256V
-
the mutant shows 59.4% activity compared to the wild type enzyme
W283A
-
the mutant shows 7.6% activity compared to the wild type enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in CHO cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, J.; Shworak, N.W.; Sinay, P.; Schwartz, J.J.; Zhang, L.; Fritze, L.M.S.; Rosenberg, R.D.
Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities
J. Biol. Chem.
274
5185-5192
1999
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Shukla, D.; Liu, J.; Blaiklock, P.; Shworak, N.W.; Bai, X.; Esko, J.D.; Cohen, G.H.; Eisenberg, R.J.; Rosenberg, R.D.; Spear, P.G.
A novel role for the 3-O-sulfated heparan sulfate in Herpes simplex virus 1 entry
Cell
99
13-22
1999
Homo sapiens, Mus musculus (Q9QZS6)
Manually annotated by BRENDA team
Moon, A.F.; Xu, Y.; Woody, S.M.; Krahn, J.M.; Linhardt, R.J.; Liu, J.; Pedersen, L.C.
Dissecting the substrate recognition of 3-O-sulfotransferase for the biosynthesis of anticoagulant heparin
Proc. Natl. Acad. Sci. USA
109
5265-5270
2012
Mus musculus
Manually annotated by BRENDA team