Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
}
TY - JOUR
T1 - Activation of ribulose 1,5-bisphosphate carboxylase by Ca2+
AU - Parry, Martin A J
AU - Schmidt, C. N Godfrey
AU - Keys, Alfred J.
AU - Gutteridge, Steven
PY - 1983/8/8
Y1 - 1983/8/8
N2 - Purified RuBP carboxylase requires activation by reaction with CO2 and a divalent metal ion. Mg2+ is the most effective metal ion, and is probably involved in activation in vivo. Ca2+ is reported not to be an activator. Several oxyanions, including phosphate esters, are effectors of activation of RuBP carboxylase by Co2 and Mg2+. It is now shown that Ca2+ is an effective activator of RuBP carboxylase and that PO4 3-, FBP, NADPH and 6-phosphogluconate are effectors of this activation. The ratio of oxygenase to carboxylase activity of enzyme activated with Ca2+ is similar to that for the enzyme activated with Mg2+.
AB - Purified RuBP carboxylase requires activation by reaction with CO2 and a divalent metal ion. Mg2+ is the most effective metal ion, and is probably involved in activation in vivo. Ca2+ is reported not to be an activator. Several oxyanions, including phosphate esters, are effectors of activation of RuBP carboxylase by Co2 and Mg2+. It is now shown that Ca2+ is an effective activator of RuBP carboxylase and that PO4 3-, FBP, NADPH and 6-phosphogluconate are effectors of this activation. The ratio of oxygenase to carboxylase activity of enzyme activated with Ca2+ is similar to that for the enzyme activated with Mg2+.
KW - 6-Phosphogluconate
KW - Activation by Ca
KW - Oxyanion effector
KW - RuBP carboxylase
UR - http://www.scopus.com/inward/record.url?scp=40849093447&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(83)80426-8
DO - 10.1016/0014-5793(83)80426-8
M3 - Journal article
AN - SCOPUS:40849093447
VL - 159
SP - 107
EP - 111
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -