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2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
bacteriochlorophyllide a + NADP+
3,8-divinyl chlorophyll a + NADPH + H+
3-monovinyl chlorophyll a + NADP+
-
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
3-vinyl-chlorophyll a + NADP+
3,8-divinyl chlorophyll a + NADPH + H+
chlorophyll a + NADP+
3,8-divinyl chlorophyllide a + NADPH + H+
3-monovinyl chlorophyllide a + NADP+
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
preferred reaction of BciA
-
-
?
8-vinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
divinyl chlorophyllide a + NADPH + H+
monovinyl chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide a + NADP+
3,8-divinyl protochlorophyllide a + NADPH + H+
-
-
-
-
?
additional information
?
-
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
?
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
strictly dependent on divinyl chlorophyllide a and NADPH, no activity with divinyl protochlorophyllide a, NADH and GSH
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
strictly dependent on divinyl chlorophyllide a and NADPH, no activity with divinyl protochlorophyllide a, NADH and GSH
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
key enzyme of the chlorophyll biosynthetic pathway
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
?
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
strictly dependent on divinyl chlorophyllide a and NADPH, no activity with divinyl protochlorophyllide a, NADH and GSH
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
strictly dependent on divinyl chlorophyllide a and NADPH, no activity with divinyl protochlorophyllide a, NADH and GSH
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
key enzyme of the chlorophyll biosynthetic pathway
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
bacteriochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
bacteriochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
3-vinyl-chlorophyll a + NADP+
-
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
3-vinyl-chlorophyll a + NADP+
-
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
chlorophyll a + NADP+
very low activity
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
chlorophyll a + NADP+
-
very low activity
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-monovinyl chlorophyllide a + NADP+
-
major substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-monovinyl chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
low activity
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
Parasynechococcus marenigrum WH 8102
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
Parasynechococcus marenigrum WH 8102
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
8-vinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
-
-
?
8-vinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
-
-
?
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
8V Chlide is the preferred substrate for BciA, with high substrate specificity
-
-
?
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate with high substrate specificity
-
-
?
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
8V Chlide is the preferred substrate for BciA, with high substrate specificity
-
-
?
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate with high substrate specificity
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
additional information
?
-
-
no activity with 3,8-divinyl chlorophyllide b and 3,8-divinyl protochlorophyllide a
-
-
?
additional information
?
-
substrate specificity, overview. 3,8-Divinylprotochlorophyllide is a poor substrate, N-DVR has a high specificity for 3,8-divinyl chlorophyllide a
-
-
?
additional information
?
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. AtDVR is able to efficiently convert 3,8-divinyl chlorophyllide a to 3-vinyl chlorophyllide a with higher reaction velocities. In addition, the AtDVR enzyme is also able to convert 3,8-divinyl protochlorophyllide a and divinyl magnesium-protoporphyrin IX monomethyl ester into monovinyl protochlorophyllide a and monovinyl magnesium-protoporphyrin IX monomethyl ester, respectively. Although the reaction velocity is extremely slow
-
-
?
additional information
?
-
the native 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. Recombinant enzyme RSBciA is active, albeit not in vivo with the engineered pathway, but shows very slow activity
-
-
?
additional information
?
-
-
the native 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. Recombinant enzyme RSBciA is active, albeit not in vivo with the engineered pathway, but shows very slow activity
-
-
?
additional information
?
-
the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway
-
-
?
additional information
?
-
-
the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway
-
-
?
additional information
?
-
the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway
-
-
?
additional information
?
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. CsDVR is able to efficiently convert 3,8-divinyl chlorophyllide a to 3-vinyl chlorophyllide a with higher reaction velocities. In addition, the CsDVR enzyme is also able to convert 3,8-divinyl protochlorophyllide a and divinyl magnesium-protoporphyrin IX monomethyl ester into monovinyl protochlorophyllide a and monovinyl magnesium-protoporphyrin IX monomethyl ester, respectively. Although the reaction velocity is extremely slow
-
-
?
additional information
?
-
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. CsDVR is able to efficiently convert 3,8-divinyl chlorophyllide a to 3-vinyl chlorophyllide a with higher reaction velocities. In addition, the CsDVR enzyme is also able to convert 3,8-divinyl protochlorophyllide a and divinyl magnesium-protoporphyrin IX monomethyl ester into monovinyl protochlorophyllide a and monovinyl magnesium-protoporphyrin IX monomethyl ester, respectively. Although the reaction velocity is extremely slow
-
-
?
additional information
?
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. Catalytic activity of OsDVR on 3,8-divinyl chlorophyllide a is about 50% higher than that on 3,8-divinyl chlorophyll a and about 160 and 320fold higher than that on 3,8-divinyl protochlorophyllide a and divinyl magnesium-protoporphyrin IX monomethyl ester, respectively
-
-
?
additional information
?
-
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. Catalytic activity of OsDVR on 3,8-divinyl chlorophyllide a is about 50% higher than that on 3,8-divinyl chlorophyll a and about 160 and 320fold higher than that on 3,8-divinyl protochlorophyllide a and divinyl magnesium-protoporphyrin IX monomethyl ester, respectively
-
-
?
additional information
?
-
-
substrate specificity, overview. Diatom N-DVR cannot convert 3,8-divinyl-protochlorophyllide a to 3-vinyl-protochlorophyllide a, but diatom N-DVR can efficiently utilize both 3,8-divinyl-chlorophyll a and 3,8-divinyl-chlorophyllide a, different from other N-DVRs, though in vitro, diatom N-DVR does not convert Chl c2 to Chl c1. No ferredoxin-dependent F-DVR activity, EC 1.3.7.13
-
-
?
additional information
?
-
-
measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction
-
-
-
additional information
?
-
measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction
-
-
-
additional information
?
-
measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction
-
-
-
additional information
?
-
measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction
-
-
-
additional information
?
-
-
measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction
-
-
-
additional information
?
-
measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. ZmDVR is able to convert all five divinyl-Chl intermediates into corresponding monovinyl compounds
-
-
?
additional information
?
-
-
substrate specificity, overview. The enzyme is also active with divinyl magnesium-protoporphyrin IX monomethyl ester and divinyl magnesium protoporphyrin IX. ZmDVR is able to convert all five divinyl-Chl intermediates into corresponding monovinyl compounds
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
bacteriochlorophyllide a + NADP+
3,8-divinyl chlorophyll a + NADPH + H+
3-vinyl-chlorophyll a + NADP+
3,8-divinyl chlorophyll a + NADPH + H+
chlorophyll a + NADP+
-
very low activity
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-monovinyl chlorophyllide a + NADP+
-
major substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
preferred reaction of BciA
-
-
?
8-vinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
3,8-divinyl protochlorophyllide a + NADPH + H+
-
-
-
-
?
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
key enzyme of the chlorophyll biosynthetic pathway
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
key enzyme of the chlorophyll biosynthetic pathway
i.e. monovinyl chlorophyllide a
r
2,4-divinyl chlorophyllide a + NADPH + H+
2-vinyl-4-ethyl chlorophyllide a + NADP+
-
-
i.e. monovinyl chlorophyllide a
r
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
bacteriochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
bacteriochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
3-vinyl-chlorophyll a + NADP+
-
-
-
?
3,8-divinyl chlorophyll a + NADPH + H+
3-vinyl-chlorophyll a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
3-vinyl-chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
low activity
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
preferred substrate
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
Parasynechococcus marenigrum WH 8102
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
3-vinyl-protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
Parasynechococcus marenigrum WH 8102
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
-
-
-
?
8-vinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
-
-
?
8-vinyl protochlorophyllide a + NADPH + H+
protochlorophyllide a + NADP+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
-
-
?
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
8V Chlide is the preferred substrate for BciA, with high substrate specificity
-
-
?
C8-vinyl chlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
8V Chlide is the preferred substrate for BciA, with high substrate specificity
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
chlorophyllide a + NADP+
divinyl chlorophyllide a + NADPH + H+
-
-
-
-
?
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evolution
either F-DVR or N-DVR is found in most photosynthetic organisms, yet both F-DVR and N-DVR exist in the genome of diatoms that contain Chl a and Chl c1
evolution
-
either F-DVR or N-DVR is found in most photosynthetic organisms, yet both F-DVR and N-DVR exist in the genome of diatoms that contain Chl a and Chl c1. Diatom N-DVR has evolved to function in Chl a biosynthesis, and diatom F-DVR is responsible for the biosynthesis of Chl c1 from Chl c2
evolution
single DVR with broad substrate specificity is responsible for reducing the 8-vinyl groups of various chlorophyll intermediates in higher plants, but DVR proteins from different species have diverse and differing substrate preferences, although they are homologous
evolution
single DVR with broad substrate specificity is responsible for reducing the 8-vinyl groups of various chlorophyll intermediates in higher plants, but DVR proteins from different species have diverse and differing substrate preferences, although they are homologous
evolution
single DVR with broad substrate specificity is responsible for reducing the 8-vinyl groups of various chlorophyll intermediates in higher plants, but DVR proteins from different species have diverse and differing substrate preferences, although they are homologous
evolution
single DVR with broad substrate specificity is responsible for reducing the 8-vinyl groups of various chlorophyll intermediates in higher plants, but DVR proteins from different species have diverse and differing substrate preferences, although they are homologous
evolution
two unrelated classes of 8-vinyl reductases are known to exist in oxygenic phototrophs, BciA and BciB. Transcript and proteomic analysis of Acaryochloris marina reveal that both bciA and bciB are expressed and their encoded proteins are present in the cell, possibly in order to ensure that all synthesized chlorophyll pigment carries an ethyl group at C-8. The presence of two 8-vinyl reductases is unique for cyanobacteria. The phylogenetic positions of Acaryochloris marina BciA and BciB are both broadly consistent with those shown for Acaryochloris marina in the 16S rRNA trees, suggesting that the bciA and bciB genes have not been acquired by horizontal transfer. However, the positions of Synechococcus spp. in the BciA tree and the clade containing the green sulfur bacteria in the BciB tree are inconsistent with the 16S rRNA phylogeny, indicating that there may have been lateral transfer events during the evolution of both bciA and bciB
evolution
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB
evolution
BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity
evolution
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments
evolution
Parasynechococcus marenigrum WH 8102
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments
evolution
-
BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity
-
evolution
-
two unrelated classes of 8-vinyl reductases are known to exist in oxygenic phototrophs, BciA and BciB. Transcript and proteomic analysis of Acaryochloris marina reveal that both bciA and bciB are expressed and their encoded proteins are present in the cell, possibly in order to ensure that all synthesized chlorophyll pigment carries an ethyl group at C-8. The presence of two 8-vinyl reductases is unique for cyanobacteria. The phylogenetic positions of Acaryochloris marina BciA and BciB are both broadly consistent with those shown for Acaryochloris marina in the 16S rRNA trees, suggesting that the bciA and bciB genes have not been acquired by horizontal transfer. However, the positions of Synechococcus spp. in the BciA tree and the clade containing the green sulfur bacteria in the BciB tree are inconsistent with the 16S rRNA phylogeny, indicating that there may have been lateral transfer events during the evolution of both bciA and bciB
-
evolution
-
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments
-
evolution
-
BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity
-
evolution
-
BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity
-
evolution
-
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB
-
malfunction
spontaneous mutant, 824ys, in rice bearing a mutation in Os03g22780 gene exhibits a yellow-green leaf phenotype, reduced chlorophyll level, arrested chloroplast development, and retarded growth rate
malfunction
-
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a
malfunction
-
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a, pigment compositions of wild-type and mutant strains, overview
malfunction
loss of 8-vinyl reductase activity in Acaryochloris marina results in the production of 8-vinyl-Chl a and 8-vinyl-Chl d with a negative effect on viability of the cells
malfunction
the bciA deletion mutant of Chlorobaculum tepidum accumulates C8V pigments. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c
malfunction
the OsDVR-inactivated 824ys mutant of rice exclusively accumulates divinyl chlorophylls in its various organs during different developmental stages
malfunction
-
the bciA deletion mutant of Chlorobaculum tepidum accumulates C8V pigments. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c
-
malfunction
-
loss of 8-vinyl reductase activity in Acaryochloris marina results in the production of 8-vinyl-Chl a and 8-vinyl-Chl d with a negative effect on viability of the cells
-
malfunction
-
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a, pigment compositions of wild-type and mutant strains, overview
-
malfunction
-
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a
-
malfunction
-
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a
-
metabolism
-
in bacteriochlorophyll a biosynthesis, the reduction of the C8 vinyl group in 8-vinyl-chlorophyllide a is catalyzed to produce chlorophyllide a by an 8-vinyl reductase called divinyl reductase (DVR), which is divided into two types, BciA and BciB. Rhodopseudomonas palustris has only BciB as its divinyl reductase DVR. Chlorophyllide a is converted into 3-vinylbacteriochlorophyllide a and then into bacteriochlorophyll a, pathway overview
metabolism
-
in bacteriochlorophyll a biosynthesis, the reduction of the C8 vinyl group in 8-vinyl-chlorophyllide a is catalyzed to produce chlorophyllide a by an 8-vinyl reductase called divinyl reductase (DVR), which is into two types, BciA and BciB. Rhodobacter sphaeroides contains BciA but no BciB, and also another distinct divinyl reductase. Chlorophyllide a oxidoreductase, COR, performs two functions: reductions of the C8 vinyl group and the C7=C8 double bond. Chlorophyllide a is converted into 3-vinylbacteriochlorophyllide a and then into bacteriochlorophyll a, pathway overview
metabolism
green bacteria like Chlorobaculum tepidum are unique in that they are able to produce different types of Chls and Bchls, and encode in their genomes several homologs (BchS, T) of the large subunit (BchH) of the magnesium chelatase, which may play a role in regulating the types of (B)Chls produced
metabolism
-
the enzyme is involved the chlorophyll biosynthetic pathways of oxygenic photosynthetic organisms. At the later steps of chlorophyll biosynthesis, 3,8-divinyl-chlorophyllide (Chlide) a is converted to monovinyl (MV)-Chlide a by DVR
metabolism
the enzyme is involved the chlorophyll biosynthetic pathways of oxygenic photosynthetic organisms. At the later steps of chlorophyll biosynthesis, 3,8-divinyl-chlorophyllide (Chlide) a is converted to monovinyl (MV)-Chlide a by DVR
metabolism
the majority of (B)Chls utilized for light-harvesting carry an ethyl group at the C8 position (8E) of the macrocycle. This group is produced by the reduction of a vinyl group (8V), catalysed by an 8V reductase, 8VR, resulting in the production of an 8E pigment. Although BciA demonstrates flexible specificity, biosynthetic heterogeneity does not occur in this organism when its preferred substrate is present, implying that, in this case, the biosynthetic pathway is linear
metabolism
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a
metabolism
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciA gene encodes the 8V reductase. BciA contains no cofactor and its reductant is NADPH
metabolism
Parasynechococcus marenigrum WH 8102
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciA gene encodes the 8V reductase. BciA contains no cofactor and its reductant is NADPH
metabolism
-
green bacteria like Chlorobaculum tepidum are unique in that they are able to produce different types of Chls and Bchls, and encode in their genomes several homologs (BchS, T) of the large subunit (BchH) of the magnesium chelatase, which may play a role in regulating the types of (B)Chls produced
-
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a
-
metabolism
-
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciA gene encodes the 8V reductase. BciA contains no cofactor and its reductant is NADPH
-
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a
-
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a
-
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a
-
metabolism
-
in bacteriochlorophyll a biosynthesis, the reduction of the C8 vinyl group in 8-vinyl-chlorophyllide a is catalyzed to produce chlorophyllide a by an 8-vinyl reductase called divinyl reductase (DVR), which is into two types, BciA and BciB. Rhodobacter sphaeroides contains BciA but no BciB, and also another distinct divinyl reductase. Chlorophyllide a oxidoreductase, COR, performs two functions: reductions of the C8 vinyl group and the C7=C8 double bond. Chlorophyllide a is converted into 3-vinylbacteriochlorophyllide a and then into bacteriochlorophyll a, pathway overview
-
metabolism
-
in bacteriochlorophyll a biosynthesis, the reduction of the C8 vinyl group in 8-vinyl-chlorophyllide a is catalyzed to produce chlorophyllide a by an 8-vinyl reductase called divinyl reductase (DVR), which is divided into two types, BciA and BciB. Rhodopseudomonas palustris has only BciB as its divinyl reductase DVR. Chlorophyllide a is converted into 3-vinylbacteriochlorophyllide a and then into bacteriochlorophyll a, pathway overview
-
metabolism
-
in bacteriochlorophyll a biosynthesis, the reduction of the C8 vinyl group in 8-vinyl-chlorophyllide a is catalyzed to produce chlorophyllide a by an 8-vinyl reductase called divinyl reductase (DVR), which is divided into two types, BciA and BciB. Rhodopseudomonas palustris has only BciB as its divinyl reductase DVR. Chlorophyllide a is converted into 3-vinylbacteriochlorophyllide a and then into bacteriochlorophyll a, pathway overview
-
metabolism
-
the majority of (B)Chls utilized for light-harvesting carry an ethyl group at the C8 position (8E) of the macrocycle. This group is produced by the reduction of a vinyl group (8V), catalysed by an 8V reductase, 8VR, resulting in the production of an 8E pigment. Although BciA demonstrates flexible specificity, biosynthetic heterogeneity does not occur in this organism when its preferred substrate is present, implying that, in this case, the biosynthetic pathway is linear
-
physiological function
divinyl reductase (DVR) converts 8-vinyl groups on various chlorophyll intermediates to ethyl groups, which is indispensable for chlorophyll biosynthesis
physiological function
divinyl reductase (DVR) converts 8-vinyl groups on various chlorophyll intermediates to ethyl groups, which is indispensable for chlorophyll biosynthesis
physiological function
divinyl reductase (DVR) converts 8-vinyl groups on various chlorophyll intermediates to ethyl groups, which is indispensable for chlorophyll biosynthesis
physiological function
divinyl reductase (DVR) converts 8-vinyl groups on various chlorophyll intermediates to ethyl groups, which is indispensable for chlorophyll biosynthesis
physiological function
functional complementation of an enzyme-deficient DELTAbciB Synechocystis sp. strain PCC 6803
physiological function
-
the enzyme is involved in the biosynthesis of bacteriochlorophyll (BChl) a in Rhodobacter sphaeroides
physiological function
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciA is an NADPH-dependent 8VR with a preference for the 8-vinyl chlorophyllide a (8 V-Chlide) substrate compared with 8-vinyl PChlide (8 V-PChlide)
physiological function
BciA is a plant-type NADPH-dependent divinyl reductase, it works for reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
physiological function
in the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria. Analysis of the enzymatic activity of cyanobacterial BciA, as well as the relationship between BciA occurrence and iron availability in cyanobacteria habitats
physiological function
Parasynechococcus marenigrum WH 8102
in the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria. Analysis of the enzymatic activity of cyanobacterial BciA, as well as the relationship between BciA occurrence and iron availability in cyanobacteria habitats
physiological function
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bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciA is an NADPH-dependent 8VR with a preference for the 8-vinyl chlorophyllide a (8 V-Chlide) substrate compared with 8-vinyl PChlide (8 V-PChlide)
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physiological function
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BciA is a plant-type NADPH-dependent divinyl reductase, it works for reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
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physiological function
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functional complementation of an enzyme-deficient DELTAbciB Synechocystis sp. strain PCC 6803
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physiological function
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in the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria. Analysis of the enzymatic activity of cyanobacterial BciA, as well as the relationship between BciA occurrence and iron availability in cyanobacteria habitats
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physiological function
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bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciA is an NADPH-dependent 8VR with a preference for the 8-vinyl chlorophyllide a (8 V-Chlide) substrate compared with 8-vinyl PChlide (8 V-PChlide)
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physiological function
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bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciA is an NADPH-dependent 8VR with a preference for the 8-vinyl chlorophyllide a (8 V-Chlide) substrate compared with 8-vinyl PChlide (8 V-PChlide)
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physiological function
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bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciA is an NADPH-dependent 8VR with a preference for the 8-vinyl chlorophyllide a (8 V-Chlide) substrate compared with 8-vinyl PChlide (8 V-PChlide)
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physiological function
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BciA is a plant-type NADPH-dependent divinyl reductase, it works for reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
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physiological function
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BciA is a plant-type NADPH-dependent divinyl reductase, it works for reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
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additional information
the enzyme encoded by gene nmrA shows 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH) activity and shall be renamed bciA
additional information
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the enzyme encoded by gene nmrA shows 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH) activity and shall be renamed bciA
additional information
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the enzyme encoded by gene nmrA shows 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH) activity and shall be renamed bciA
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additional information
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construction of a bchXYZ deletion mutant, construction of a Rhodobacter palustris bciA mutant. The mutant lacking sole BciA can grow under anaerobic light conditions as well as aerobic dark conditions. On the other hand, the single bchXYZ mutant and the double bciA/bchXYZ mutant do not show phototrophic growth and grow under aerobic/semiaerobic conditions in the dark
additional information
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a strain of Rhodobacter sphaeroides mutant lacking BchJ and BciA with incorporated bchYZ of bacteriochlorophyll b-producing Blastochloris viridis, encoding chlorophyllide a oxidoreductase (COR), shows accumulating of both BChla and BChlb and becomes an anoxygenic photosynthetic bacterium producing BChls a and b together. Loss of functions of both intrinsic COR and 8-vinyl reductase (BciA) in the host and expression of the BchYZ catalytic components of COR from Blastochloris viridis, not the complete set of COR (BchXYZ), is essential for production of bacteriochlorophylls a and b in the host strain
additional information
engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. RSBciA is completely inactive in our recombinant system. RSBciA is completely inactive in our recombinant system. Subcloning in Escherichia coli strain JM109
additional information
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engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. RSBciA is completely inactive in our recombinant system. RSBciA is completely inactive in our recombinant system. Subcloning in Escherichia coli strain JM109
additional information
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construction of a bchXYZ deletion mutant, construction of a Rhodobacter palustris bciA mutant. The mutant lacking sole BciA can grow under anaerobic light conditions as well as aerobic dark conditions. On the other hand, the single bchXYZ mutant and the double bciA/bchXYZ mutant do not show phototrophic growth and grow under aerobic/semiaerobic conditions in the dark
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additional information
construction of mutant tepdA lacking enzymes BciA and BchU, that catalyze reduction of the C8-vinyl group and methylation at the C20 position of bacteriochlorophyll (BChl) c, respectively, in the green sulfur bacterium Chlorobaculum tepidum, the mutant accumula C8-vinyl-bacteriochlorophyllide d derivative, determined by NMR to be (31R)-8-vinyl-12-ethyl-(R[V,E])BChl d. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c. Reconstitution of self-aggregates of C8V-BChl species in vitro. Comparison of chlorophyllide a derivatives in tepdA strains lacking bciA and/or bciU, overview
additional information
engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. No mono-vinyl forms of any of the pathway intermediates upon coexpression of the 8-vinyl reductase with BchSID and BchM. PIX overproducing cells expressing BchSID and CTBciA alone produce two additional compounds, mono-vinyl PIX (mvPIX) and mono-vinyl MgPIX (mvMgPIX), indicating that CTBciA is capable of reducing the C8-vinyl group on both the Mg chelated and the non-Mg chelated porphyrin molecule
additional information
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engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. No mono-vinyl forms of any of the pathway intermediates upon coexpression of the 8-vinyl reductase with BchSID and BchM. PIX overproducing cells expressing BchSID and CTBciA alone produce two additional compounds, mono-vinyl PIX (mvPIX) and mono-vinyl MgPIX (mvMgPIX), indicating that CTBciA is capable of reducing the C8-vinyl group on both the Mg chelated and the non-Mg chelated porphyrin molecule
additional information
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construction of mutant tepdA lacking enzymes BciA and BchU, that catalyze reduction of the C8-vinyl group and methylation at the C20 position of bacteriochlorophyll (BChl) c, respectively, in the green sulfur bacterium Chlorobaculum tepidum, the mutant accumula C8-vinyl-bacteriochlorophyllide d derivative, determined by NMR to be (31R)-8-vinyl-12-ethyl-(R[V,E])BChl d. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c. Reconstitution of self-aggregates of C8V-BChl species in vitro. Comparison of chlorophyllide a derivatives in tepdA strains lacking bciA and/or bciU, overview
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additional information
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engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. No mono-vinyl forms of any of the pathway intermediates upon coexpression of the 8-vinyl reductase with BchSID and BchM. PIX overproducing cells expressing BchSID and CTBciA alone produce two additional compounds, mono-vinyl PIX (mvPIX) and mono-vinyl MgPIX (mvMgPIX), indicating that CTBciA is capable of reducing the C8-vinyl group on both the Mg chelated and the non-Mg chelated porphyrin molecule
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additional information
generation of the OsDVR-inactivated 824ys mutant of rice that shows no DVR activity
additional information
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generation of the OsDVR-inactivated 824ys mutant of rice that shows no DVR activity
additional information
Parasynechococcus marenigrum WH 8102
BciA and BciB can be readily exchanged, and BciA can be efficiently transferred to cyanobacteria
additional information
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construction of a bchXYZ deletion mutant, construction of a Rhodobacter palustris bciB mutant using the plasmid pJSC-palB-Km
additional information
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construction of a bchXYZ deletion mutant, construction of a Rhodobacter palustris bciB mutant using the plasmid pJSC-palB-Km
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additional information
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construction of a bchXYZ deletion mutant, construction of a Rhodobacter palustris bciB mutant using the plasmid pJSC-palB-Km
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Tripathy, B.C.; Rebeiz, C.A.
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153
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Oryza sativa (D5L1S4), Oryza sativa (Q10LH0), Oryza sativa
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Harada, J.; Mizoguchi, T.; Tsukatani, Y.; Yokono, M.; Tanaka, A.; Tamiaki, H.
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis
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Cereibacter sphaeroides, Rhodopseudomonas palustris, Cereibacter sphaeroides J001, Rhodopseudomonas palustris J002
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The major route for chlorophyll synthesis includes [3,8-divinyl]-chlorophyllide a reduction in Arabidopsis thaliana
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Canniffe, D.P.; Chidgey, J.W.; Hunter, C.N.
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Cereibacter sphaeroides (Q3IXP7), Cereibacter sphaeroides, Cereibacter sphaeroides DSM 158 (Q3IXP7)
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Chen, G.E.; Hitchcock, A.; Jackson, P.J.; Chaudhuri, R.R.; Dickman, M.J.; Hunter, C.N.; Canniffe, D.P.
Two unrelated 8-vinyl reductases ensure production of mature chlorophylls in Acaryochloris marina
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Harada, J.; Mizoguchi, T.; Nomura, K.; Tamiaki, H.
Isolation and structural determination of C8-vinyl-bacteriochlorophyll d from the bciA and bchU double mutant of the green sulfur bacterium Chlorobaculum tepidum
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2013
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A tale of two reductases extending the bacteriochlorophyll biosynthetic pathway in E. coli
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Distribution and functional analysis of the two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria
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203
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Mizoguchi, T.; Kinoshita, Y.; Harada, J.; Ogasawara, S.; Tamiaki, H.
Light-dependent accumulation of new bacteriochlorophyll-e bearing a vinyl group at the 8-position in the green sulfur bacterium Chlorobaculum limnaeum
J. Photochem. Photobiol. A
358
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Chlorobaculum limnaeum
brenda