PMID- 10207017
OWN - NLM
STAT- MEDLINE
DCOM- 19990520
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 17
DP  - 1999 Apr 23
TI  - Molecular cloning and functional expression of two members of mouse
      NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2,6-sialyltransferase family, ST6GalNAc 
      III and IV.
PG  - 11958-67
AB  - Two cDNA clones encoding NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2,
      6-sialyltransferase have been isolated from mouse brain cDNA libraries. One of
      the cDNA clones is a homologue of previously reported rat ST6GalNAc III according
      to the amino acid sequence identity (94.4%) and the substrate specificity of the 
      expressed recombinant enzyme, while the other cDNA clone includes an open reading
      frame coding for 302 amino acids. The deduced amino acid sequence is not
      identical to those of other cloned mouse sialyltransferases, although it shows
      the highest sequence similarity with mouse ST6GalNAc III (43.0%). The expressed
      soluble recombinant enzyme exhibited activity toward NeuAcalpha2, 3Galbeta1,
      3GalNAc, fetuin, and GM1b, while no significant activity was detected toward
      Galbeta1,3GalNAc or asialofetuin, or the other glycoprotein substrates tested.
      The sialidase sensitivity of the 14C-sialylated residue of fetuin, which was
      sialylated by this enzyme with CMP-[14C]NeuAc, was the same as that of ST6GalNAc 
      III. These results indicate that the expressed enzyme is a new type of
      GalNAcalpha2,6-sialyltransferase, which requires sialic acid residues linked to
      Galbeta1,3GalNAc residues for its activity; therefore, we designated it mouse
      ST6GalNAc IV. Although the substrate specificity of this enzyme is similar to
      that of ST6GalNAc III, ST6GalNAc IV prefers O-glycans to glycolipids.
      Glycolipids, however, are better substrates for ST6GalNAc III.
FAU - Lee, Y C
AU  - Lee YC
AD  - Molecular Glycobiology, Frontier Research Program, Institute of Physical and
      Chemical Research (RIKEN), Wako, Saitama 351-0198, Japan.
FAU - Kaufmann, M
AU  - Kaufmann M
FAU - Kitazume-Kawaguchi, S
AU  - Kitazume-Kawaguchi S
FAU - Kono, M
AU  - Kono M
FAU - Takashima, S
AU  - Takashima S
FAU - Kurosawa, N
AU  - Kurosawa N
FAU - Liu, H
AU  - Liu H
FAU - Pircher, H
AU  - Pircher H
FAU - Tsuji, S
AU  - Tsuji S
LA  - eng
SI  - GENBANK/AJ007310
SI  - GENBANK/Y11274
SI  - GENBANK/Y11339
SI  - GENBANK/Y11341
SI  - GENBANK/Y11342
SI  - GENBANK/Y15779
SI  - GENBANK/Y15780
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - EC 2.4.99.- (Neu5Ac N-acetylgalactosamine 2,6-sialyltransferase)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.7 (Siat7d protein, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Brain/enzymology
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - RNA, Messenger/genetics
MH  - Rats
MH  - Sialyltransferases/*genetics/metabolism
MH  - Substrate Specificity
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1074/jbc.274.17.11958 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 23;274(17):11958-67. doi: 10.1074/jbc.274.17.11958.