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{{enzyme
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| Name = beta-galactoside alpha-2,3-sialyltransferase
| EC_number = 2.4.99.4
| CAS_number = 71124-51-1
| IUBMB_EC_number = 2/4/99/4
| GO_code = 0003836
| image =
| width =
| caption =
}}
In [[enzymology]], a '''beta-galactoside alpha-2,3-sialyltransferase''' ({{EC number|2.4.99.4}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R <math>\rightleftharpoons</math> CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D- galactosaminyl-R
 
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[CMP-N-acetylneuraminate]] and [[beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R]], whereas its 3 [[product (chemistry)|products]] are [[cytidine monophosphate|CMP]], [[alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-]], and [[galactosaminyl-R]].
 
This enzyme belongs to the family of [[transferase]]s, specifically those [[glycosyltransferase]]s that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is '''CMP-N-acetylneuraminate:beta-D-galactoside alpha-2,3-N-acetylneuraminyl-transferase'''. This enzyme participates in 7 [[metabolism|metabolic pathways]]: [[o-glycan biosynthesis]], [[keratan sulfate biosynthesis]], [[glycosphingolipid biosynthesis - lactoseries]], [[glycosphingolipid biosynthesis - globoseries]], [[glycosphingolipid biosynthesis - ganglioseries]], [[glycan structures - biosynthesis 1]], and [[glycan structures - biosynthesis 2]].
 
==Structural studies==
 
As of late 2007, 9 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|2EX0}}, {{PDB link|2EX1}}, {{PDB link|2IHJ}}, {{PDB link|2IHK}}, {{PDB link|2IHZ}}, {{PDB link|2II6}}, {{PDB link|2IIB}}, {{PDB link|2IIQ}}, and {{PDB link|2ILV}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = Rearick JI, Sadler JE, Paulson JC, Hill RL | year = 1979 | title = Enzymatic characterization of beta D-galactoside alpha2 leads to 3 sialyltransferase from porcine submaxillary gland | journal = J. Biol. Chem. | volume = 254 | pages = 4444&ndash;51  | pmid = 438198 | issue = 11 }}
* {{cite journal | author = Sadler JE, Rearick JI, Paulson JC, Hill RL | year = 1979 | title = Purification to homogeneity of a beta-galactoside alpha2 leads to 3 sialyltransferase and partial purification of an alpha-N-acetylgalactosaminide alpha2 leads to 6 sialyltransferase from porcine submaxillary glands | journal = J. Biol. Chem| volume = 254 | pages = 4434&ndash;42  | pmid = 438196 | issue = 11 }}
 
[[Category:EC 2.4.99]]
[[Category:Enzymes of known structure]]
 
 
{{enzyme-stub}}

Revision as of 22:27, 17 March 2013

Template:Enzyme In enzymology, a beta-galactoside alpha-2,3-sialyltransferase (Air Transportation Experts Kull from Wingham, has many interests that include butterflies, property developers in singapore and digital photography. Is a travel freak and in recent past made buy a house in singapore journey to Paleochristian and Byzantine Monuments of Thessalonika.) is an enzyme that catalyzes the chemical reaction

CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D- galactosaminyl-R

Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-, and galactosaminyl-R.

This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:beta-D-galactoside alpha-2,3-N-acetylneuraminyl-transferase. This enzyme participates in 7 metabolic pathways: o-glycan biosynthesis, keratan sulfate biosynthesis, glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - globoseries, glycosphingolipid biosynthesis - ganglioseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

References

43 year old Petroleum Engineer Harry from Deep River, usually spends time with hobbies and interests like renting movies, property developers in singapore new condominium and vehicle racing. Constantly enjoys going to destinations like Camino Real de Tierra Adentro.

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Template:Enzyme-stub