Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • White, T.; Bennett, E.P.; Takio, K.; Sorensen, T.; Bonding, N.; Clausen, H.
    Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (1995), J. Biol. Chem., 270, 24156-24165.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.4.1.41 drug development further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use Homo sapiens
2.4.1.41 drug development further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for our insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.41 PCR cloning of human version of GalNAc-T1, based on the reported sequence of bovine GalNAc-T1. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level is found Homo sapiens
2.4.1.41 PCR construct is expressed in insect cells using a baculovirus vector. Expression of GalNAc-T2 in Sf9 cells Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.41 cytoplasm
-
 Homo sapiens 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.41 52000
-
 single band, SDS-PAGE. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level is found Homo sapiens
2.4.1.41 59210
-
 molecular mass of the deduced amino acid sequence of the soluble transferase is 59205 Da, which is slightly higher than the experimentally determined molecular weight but within the limits of accuracy of the SDS-PAGE and gel filtration systems used Homo sapiens
2.4.1.41 64700
-
 cDNA sequence has a 571-amino acid coding region indicating a protein of 64.7 kDa with a type II domain structure Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.41 Homo sapiens Q10471
-
-
2.4.1.41 Homo sapiens Q10472
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.41 purified to apparent homogeneity using a synthetic acceptor peptide as affinity ligand Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.41 brain Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 heart Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 kidney Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 liver Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 lung Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 MKN-45 cell gastric cancer cell line, cDNA encoding the transferase is cloned and sequenced from a cDNA library of a human cancer cell line Homo sapiens
-
2.4.1.41 pancreas Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 placenta
-
 Homo sapiens
-
2.4.1.41 placenta Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-
2.4.1.41 skeletal muscle Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.41 0.75
-
 purification step 5, Mono S (NaCl) Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.41 UDP-N-acetyl-D-galactosamine + PRFQDSSSSKAPPPSLPSPSRL
-
 Homo sapiens UDP + N-actetyl-D-galactosaminylated PRFQDSSSSKAPPPSLPSPSRL
-
 ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + PTTTPISTTMVTPTPTPTC
-
 Homo sapiens UDP + N-actetyl-D-galactosaminylated PTTTPISTTMVTPTPTPTC
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.41 GalNAc-T1 data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members Homo sapiens
2.4.1.41 GalNAc-T2 data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members Homo sapiens
2.4.1.41 GalNAc-transferase
-
 Homo sapiens
2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
 Homo sapiens