TY - JOUR
T1 - Studies of sulfate utilization by algae 13. Adenosine 5′-phosphosulfate (APS) as an intermediate in the conversion of adenosine 3′-phosphate 5′-phosphosulfate (PAPS) to acid-volatile radioactivity
AU - Goldschmidt, Eliezer E.
AU - Tsang, Monica Lik Shing
AU - Schiff, Jerome A.
PY - 1975/5
Y1 - 1975/5
N2 - An intermediate, identified as adenosine 5′-phosphosulfate (APS), has been found in the enzymatic conversion of PAP35S to acid-volatile radioactivity by enzyme fractions "A" and "S" from Chlorella pyrenoidosa. "A" was found to be a Mg2+-dependent 3′-nucleotidase specific for 3′5′-diphosphonucleosides which converts adenosine 3′-phosphate 5′-phosphosulfate (PAPS) to APS. Authentic AP35S is a substrate for "S" and yields acid-volatile radioactivity in the presence of Mg2+ and a thiol. This is of some interest since Chlorella is an assimilatory sulfate reducer and APS has been reported as a substrate only for dissimilatory sulfate reduction. PAPS production is undoubtedly concerned with providing a source of active sulfate for esterification reactions, but since fraction "A" can convert PAPS to APS, this may be yet another mechanism for forming APS despite the unfavorable equilibrium of the ATP sulfurylase reaction.
AB - An intermediate, identified as adenosine 5′-phosphosulfate (APS), has been found in the enzymatic conversion of PAP35S to acid-volatile radioactivity by enzyme fractions "A" and "S" from Chlorella pyrenoidosa. "A" was found to be a Mg2+-dependent 3′-nucleotidase specific for 3′5′-diphosphonucleosides which converts adenosine 3′-phosphate 5′-phosphosulfate (PAPS) to APS. Authentic AP35S is a substrate for "S" and yields acid-volatile radioactivity in the presence of Mg2+ and a thiol. This is of some interest since Chlorella is an assimilatory sulfate reducer and APS has been reported as a substrate only for dissimilatory sulfate reduction. PAPS production is undoubtedly concerned with providing a source of active sulfate for esterification reactions, but since fraction "A" can convert PAPS to APS, this may be yet another mechanism for forming APS despite the unfavorable equilibrium of the ATP sulfurylase reaction.
UR - http://www.scopus.com/inward/record.url?scp=0010562627&partnerID=8YFLogxK
U2 - 10.1016/0304-4211(75)90101-7
DO - 10.1016/0304-4211(75)90101-7
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AN - SCOPUS:0010562627
SN - 0304-4211
VL - 4
SP - 293
EP - 299
JO - Plant Science Letters
JF - Plant Science Letters
IS - 5
ER -