Potential use of sugar binding proteins in reactors for regeneration of CO2 fixation acceptor D-Ribulose-1,5-bisphosphate

Mahato, Sourav; De, Debojyoti; Dutta, Debajyoti; Kundu, Moloy; Bhattacharya, Sumana; Schiavone, Marc T; Bhattacharya, Sanjoy K

doi:10.1186/1475-2859-3-7

Table 4 Enzymes that bind D-Ribulose-1,5-bisphosphate

From: Potential use of sugar binding proteins in reactors for regeneration of CO₂ fixation acceptor D-Ribulose-1,5-bisphosphate

Source organism	Mutation	Remarks	References
Rubisco
Chamydomonas reinhardtii	C256F, K258R, L265V	85% decrease in Catalytic efficiency (V_max/Km)	114
Chamydomonas reinhardtii	G54V	83% decrease in the carboxylation-V_max	115
Anacystis nidulans	L339F, A340L, S341M	Decrease in Kcat and (V_max/Km) by 90%and 36.3% respectively	116
Anacystis nidulans	T342I, K343L	Decrease in Kcat and (V_max/Km) by 90%and 36.3% respectively	116
Anacystis nidulans	T342I	Decrease in Kcat and (V_max/Km) 40.5%and 40.5% respectively	116
Anacystis nidulans	K343L	Decrease in Kcat and (V_max/Km) 48.1%and 18.5% respectively	116
Anacystis nidulans	V346Y, D347H, L348T	Inactive	116
Anacystis nidulans	L326I	Decrease in Kcat and (V_max/Km) 54.4%and 34.2% respectively	116
Anacystis nidulans	S328A	Decrease in Kcat and (V_max/Km) 5.6%and 41.5% respectively	116
Anacystis nidulans	N123H	16.5% decrease in Kcat	116
Anacystis nidulans	L332M, L332I	>65% decrease in carboxylase but not in oxygenase activity	117
Anacystis nidulans		>65% decrease in carboxylase but not in oxygenase activity	117
Anacystis nidulans	L332V	67% decrease in specificity factor (CO₂/O₂)	117
Anacystis nidulans	L332T	67% decrease in specificity factor (CO₂/O₂)	117
Anacystis nidulans	L332A	>65% decrease in specificity and carboxylase activity	117
Rhodospirillum rubrum	deleation of F327	99.5% decrease in carboxylase activity	118
Rhodospirillum rubrum	F327L	Increase in Km (RuBP)	118
Rhodospirillum rubrum	F327V	Increase in Km (RuBP)	118
Rhodospirillum rubrum	F327A	Increase in Km (RuBP)	118
Rhodospirillum rubrum	F327G	165-fold increase in Km (RuBP)	118
Rhodospirillum rubrum	N111G	Km(RuBP), kcat are 320 fold increased and 88-fold decreased	119
Rhodospirillum rubrum	N111L	Mutant show a very low carboxylase activity	119
Rhodospirillum rubrum	N111Q	Mutant show a very low carboxylase activity	119
Rhodospirillum rubrum	N111B	Mutant show a very low carboxylase activity	119
Synechococcus sp. PCC6301	I87V	Mutant show a very low carboxylase activity (kcat = 35%)	120
Synechococcus sp. PCC6301	R88K	Mutant show a very low carboxylase activity (kcat = 35%)	120
Synechococcus sp. PCC6301	G91V	Mutant show a very low carboxylase activity (kcat = 35%)	120
Synechococcus sp. PCC6301	F92L	Mutant show a very low carboxylase activity (kcat = 35%)	120
Synechococcus sp. PCC6803	C172A	40–60% decline in Rubisco turnover number	121
Chlamydomonas reinhardtii	N123G	Decrease in specificity factor	122
Chlamydomonas reinhardtii	S379A	Decrease in specificity factor	122
Anacystis nidulans	S376 C	99% and ~99.9% decrease in carboxylase and oxygenase activity	123
Anacystis nidulans	S376T	99% and ~99.9% decrease in carboxylase and oxygenase activity	123
Anacystis nidulans	S376 A	99% and ~16% decrease in carboxylase and oxygenase activity	123
Rhodospirillum rubrum	I164T	6% decrease in carboxylase activity with 40-fold lower Kcat/Km	124
Rhodospirillum rubrum	I164N	1% decrease in carboxylase activity with 900-fold lower Kcat/Km	124
Rhodospirillum rubrum	I164B	0.01–1% decrease in carboxylase activity	124
Rhodospirillum rubrum	H287N	10³-fold decrase in carboxylation catalysis	125
Rhodospirillum rubrum	H287Q	10⁵-fold decrase in carboxylation catalysis	125
Rhodospirillum rubrum	M330L		126
Rubisco (large subunit)
Chamydomonas reinhardtii	R59A	Decrease in V_max for carboxylation reaction	127
Chamydomonas reinhardtii	Y67A	Decrease in V_max for carboxylation reaction	127
Chamydomonas reinhardtii	Y68A	Decrease in V_max for carboxylation reaction	127
Chamydomonas reinhardtii	D69A	Decrease in V_max for carboxylation reaction	127
Chamydomonas reinhardtii	R71A	decrease in V_max (for carboxylation reaction) and thermal stability	127
Chamydomonas reinhardtii	A222T, V262L, L290F	Improved specificity factor and thermal stability	128
Phosphoribulokinase
Rhodobacter sphaeroides	T18A	8-fold decrease in V_max	129
Rhodobacter sphaeroides	S14A	40-fold decrease in V_max	129
Rhodobacter sphaeroides	S19A	500-fold and >1500-fold decrease in V_max and V_max/Km of RuBP	129
Rhodobacter sphaeroides	K165M, K165C	10³-fold decrease in catalytic activity	130
Rhodobacter sphaeroides	R168Q	>300-fold decrease in catalytic efficiency	131
Rhodobacter sphaeroides	R173Q	15-fold decrease in V_max, 100-fold increase in Km for RuBP	131
Chlamydomonas reinhardtii	R64C	Almost inactive	132
Chlamydomonas reinhardtii	R64A	Decrease in activity	132
Chlamydomonas reinhardtii	R64K	Decrease in activity	132
Synechocystis sp.	S222F	Retains one-tenth catalytic activity	133
Rhodobacter sphaeroides	H45N	40-fold increase in Km for RuBP	134
Rhodobacter sphaeroides	N49Q	200-fold increase in Km for RuBP	134
Rhodobacter sphaeroides	K53M	No effect on catalysis or substrate binding	134
Rhodobacter sphaeroides	D169A	V_max diminished by 4-orders of magnitude	135
Rhodobacter sphaeroides	D42A	V_max diminished by 5-orders of magnitude	135
Rhodobacter sphaeroides	D42N	V_max diminished by 5-orders of magnitude	135
Rhodobacter sphaeroides	R31A	Unlike wild-type, shows hyperbolic kinetics for ATP and NADH	136

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ISSN: 1475-2859

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