PMID- 10503886
OWN - NLM
STAT- MEDLINE
DCOM- 19991012
LR  - 20061115
IS  - 0304-3835 (Print)
IS  - 0304-3835 (Linking)
VI  - 143
IP  - 2
DP  - 1999 Sep 1
TI  - Sulfotransferase catalyzing sulfation of heterocyclic amines.
PG  - 103-7
AB  - Cytosolic sulfation of arylamines to form sulfamates is found to be mediated by
      sulfotransferases of three gene families (SULT1 to 3). Among them, a SULT3 form
      (ST3A1) showed a high selectivity for N-sulfation of N-substituted aryl and
      alicyclic compounds. SULT1 (phenol) and SULT2 (hydroxysteroid) sulfotransferases 
      showed N-sulfating activities of carcinogenic heterocyclic amines. For
      N-hydroxyarylamine O-sulfation, SULT1 forms showed high activity. In rats, ST1C1 
      mediated the metabolic activation of N-hydroxyarylamines. However, the related
      form (ST1C2) in humans showed the negligible activity. Instead, ST1A3 showed high
      metabolic activating abilities among human sulfotransferases.
FAU - Yamazoe, Y
AU  - Yamazoe Y
AD  - Division of Drug Metabolism and Molecular Toxicology, Faculty of Pharmaceutical
      Sciences, Tohoku University, Sendai, Japan.
FAU - Nagata, K
AU  - Nagata K
FAU - Yoshinari, K
AU  - Yoshinari K
FAU - Fujita, K
AU  - Fujita K
FAU - Shiraga, T
AU  - Shiraga T
FAU - Iwasaki, K
AU  - Iwasaki K
LA  - eng
PT  - Journal Article
PL  - Ireland
TA  - Cancer Lett
JT  - Cancer letters
JID - 7600053
RN  - 0 (Amines)
RN  - EC 2.8.2.- (Sulfotransferases)
SB  - IM
MH  - Amines/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Catalysis
MH  - Enzyme Activation
MH  - Humans
MH  - Molecular Sequence Data
MH  - Rats
MH  - Sequence Alignment
MH  - Substrate Specificity
MH  - Sulfotransferases/*metabolism
EDAT- 1999/09/30 00:00
MHDA- 1999/09/30 00:01
CRDT- 1999/09/30 00:00
PHST- 1999/09/30 00:00 [pubmed]
PHST- 1999/09/30 00:01 [medline]
PHST- 1999/09/30 00:00 [entrez]
AID - S0304383599001366 [pii]
PST - ppublish
SO  - Cancer Lett. 1999 Sep 1;143(2):103-7.