Synthesis (Fig. 3). There is no clear differentiation that would explain the near-complete conversion of -carotene to zeaxanthin by -carotene hydroxylase (CrtR), the enzyme responsible for zeaxanthin biosynthesis. We suggest a putative carotene biosynthesis pathway (Fig. 3) that accommodates the distinct complement of the carotenoid biosynthesis enzymes and their end products in A. marina.Light-Ha
Synthesis (Fig. 3). There is no clear differentiation that would explain the near-complete conversion of -carotene to zeaxanthin by -carotene hydroxylase (CrtR), the enzyme responsible for zeaxanthin biosynthesis. We suggest a putative carotene biosynthesis pathway (Fig. 3) that accommodates the distinct complement of the carotenoid biosynthesis enzymes and their end products in A. marina.Light-Ha
Induced responses.NIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptConclusionsInfluenza infection triggers a robust B cell response in the lymphoid tissues of the respiratory tract that provides immune protection from both primary and secondary infections. The regulation of this B cell response highlights the complexities of humoral response induction and maintenance to re
Induced responses.NIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptConclusionsInfluenza infection triggers a robust B cell response in the lymphoid tissues of the respiratory tract that provides immune protection from both primary and secondary infections. The regulation of this B cell response highlights the complexities of humoral response induction and maintenance to re
Induced responses.NIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptConclusionsInfluenza infection triggers a robust B cell response in the lymphoid tissues of the respiratory tract that provides immune protection from both primary and secondary infections. The regulation of this B cell response highlights the complexities of humoral response induction and maintenance to re
Ecies (32). Such enzymes could provide another means for Chl d biosynthesis. A. marina codes for 12 proteins with putative radical SAM motifs, far more than expected from an oxygen-producing cyanobacterium. Of these 12, two (AM1 5023 and AM1 5798) share very little homology with other sequenced cyanobacteria. The Chl d biosynthesis pathway may not be as simple as expected. Unlike the formyl side c
Ecies (32). Such enzymes could provide another means for Chl d biosynthesis. A. marina codes for 12 proteins with putative radical SAM motifs, far more than expected from an oxygen-producing cyanobacterium. Of these 12, two (AM1 5023 and AM1 5798) share very little homology with other sequenced cyanobacteria. The Chl d biosynthesis pathway may not be as simple as expected. Unlike the formyl side c
Ecies (32). Such enzymes could provide another means for Chl d biosynthesis. A. marina codes for 12 proteins with putative radical SAM motifs, far more than expected from an oxygen-producing cyanobacterium. Of these 12, two (AM1 5023 and AM1 5798) share very little homology with other sequenced cyanobacteria. The Chl d biosynthesis pathway may not be as simple as expected. Unlike the formyl side c