Team:ULaval/Basic Part

Basic Parts

Part BBa_K2672000: Th

This basic part is the budding yeast codon-optimized gene that code for the human Tyrosine hydroxylase (Th): EC1.14.16.1. Th catalyzes the biochemical reaction of the transformation of L-tyrosine into L-DOPA. This reaction also requires dioxygen and tetrahydrobiopterin. Moreover, the enzyme uses the iron cations as cofactors. This is the first step of the biosynthesis of adrenaline.

The crystallographic structure is already available on the Uniprot database: P07101. The protein is a homotetramer within which each peptidic chain complexes an iron cation.

ATGCCAACTCCCGATGCTACGACACCTCAGGCTAAAGGGTTCAGGCGTGCTGTAAGCGAGTTAGATGCGAAACAAGCAGAAGCAATTATGGTCAGGGGGCAGGGGGCACCCGGTCCGTCATTGACTGGTAGCCCATGGCCCGGAACAGCAGCGCCTGCCGCCAGTTACACTCCAACACCACGTTCCCCAAGGTTTATAGGCCGTAGACAATCTTTGATCGAGGACGCTAGAAAGGAAAGGGAGGCGGCTGTGGCGGCGGCTGCTGCTGCGGTCCCCAGCGAGCCCGGAGATCCCCTTGAGGCAGTAGCATTTGAAGAGAAGGAGGGGAAGGCCGTCTTGAACTTACTTTTCTCTCCCAGGGCAACAAAGCCAAGTGCCTTGTCCAGAGCAGTGAAGGTCTTTGAAACTTTCGAGGCAAAGATTCATCATCTTGAAACGAGGCCAGCACAGCGTCCGCGTGCAGGAGGGCCGCATCTGGAGTACTTCGTGAGGCTGGAAGTTCGTAGGGGTGATCTTGCCGCGTTGCTGTCTGGAGTGCGTCAAGTGAGTGAAGATGTGCGTAGCCCAGCAGGACCTAAAGTACCATGGTTCCCACGTAAAGTGAGTGAGTTGGACAAATGTCACCATTTAGTGACAAAATTCGACCCGGATCTGGACCTGGATCATCCTGGGTTCAGCGACCAAGTGTACAGGCAAAGGCGTAAGCTAATTGCAGAAATTGCCTTCCAGTACAGGCACGGGGATCCGATTCCTAGAGTTGAGTACACGGCTGAGGAAATCGCCACTTGGAAAGAGGTGTACACGACTTTAAAGGGCTTGTACGCAACACATGCCTGTGGTGAACATTTGGAGGCTTTTGCGCTGCTTGAGAGATTTTCTGGCTACAGGGAGGATAATATCCCGCAATTAGAGGACGTGAGCAGGTTTCTAAAGGAGAGGACAGGGTTTCAGTTAAGACCTGTGGCGGGGTTGTTGTCAGCAAGGGATTTCCTAGCCTCCCTAGCTTTCCGTGTCTTTCAATGTACCCAATATATTAGGCACGCGAGTTCACCCATGCATAGTCCGGAACCAGATTGCTGTCATGAGTTACTTGGTCATGTTCCGATGCTGGCAGATAGAACGTTTGCACAGTTCAGCCAGGATATAGGCCTTGCTTCTTTAGGGGCCTCTGACGAGGAGATCGAGAAGTTAAGTACTTTGTATTGGTTCACGGTGGAATTTGGACTTTGCAAACAAAATGGTGAGGTGAAGGCCTACGGTGCCGGACTATTATCTAGTTACGGAGAGTTGTTGCACTGCCTGTCTGAGGAACCGGAGATCCGTGCGTTTGACCCCGAGGCCGCGGCGGTTCAGCCCTACCAAGATCAAACATATCAGTCAGTATACTTCGTCTCCGAGAGTTTTAGCGATGCCAAGGACAAGTTACGTTCTTACGCCTCCAGAATACAACGTCCATTTAGCGTCAAATTTGATCCGTATACCTTAGCGATAGACGTCTTGGACTCTCCGCAGGCCGTTAGAAGAAGCCTTGAAGGGGTACAAGATGAATTAGACACATTGGCCCATGCTCTGTCAGCGATCGGTTGA

Part BBa_K2672001: LDDC

This basic part is the budding yeast codon-optimized gene that encodes the human L-DOPA decarboxylase: EC4.1.1.28. This enzyme catalyzes the decarboxylation reaction of L-DOPA to form a dopamine molecule. The enzyme uses the iron cations as cofactors. This is the second step of the biosynthesis of adrenaline.

LDDC is a tightly associated α2-dimer within which each of the two monomers is composed of three distinct domains. The active site of LDDC is located near the monomer-monomer interface but is mainly composed of residues from one monomer¹.

ATGAATGCGTCTGAGTTCCGTCGTAGGGGGAAGGAGATGGTGGATTACATGGCAAACTATATGGAAGGCATAGAGGGAAGACAAGTTTATCCTGATGTGGAACCAGGTTATCTACGTCCTCTAATTCCTGCGGCAGCCCCGCAGGAGCCAGATACATTTGAGGACATTATCAATGATGTAGAGAAGATAATTATGCCTGGCGTTACGCATTGGCACAGTCCTTACTTCTTTGCCTATTTTCCCACAGCATCTTCTTACCCGGCTATGCTGGCAGATATGTTGTGCGGCGCCATTGGATGCATCGGCTTCTCCTGGGCCGCCAGCCCGGCCTGCACTGAATTGGAGACAGTAATGATGGACTGGCTTGGAAAGATGCTAGAGCTACCGAAAGCATTCTTAAATGAAAAGGCCGGCGAAGGAGGAGGGGTTATTCAGGGTAGCGCTTCTGAAGCGACGTTAGTAGCATTATTAGCGGCAAGAACGAAAGTTATACATAGACTACAGGCCGCGAGTCCGGAACTAACACAGGCCGCAATCATGGAAAAGCTAGTCGCCTACTCCTCCGACCAAGCCCACTCATCAGTAGAACGTGCAGGTCTGATAGGTGGAGTTAAGTTGAAGGCGATACCCTCCGACGGGAACTTTGCAATGCGTGCTTCCGCCTTACAGGAAGCATTGGAGCGTGACAAAGCGGCTGGATTGATACCTTTTTTTATGGTAGCCACATTGGGAACCACGACCTGCTGCTCATTTGACAATCTATTGGAAGTCGGGCCGATATGTAACAAAGAAGACATATGGCTTCATGTCGATGCAGCATACGCGGGATCTGCCTTCATATGTCCAGAGTTCCGTCATCTTCTGAATGGAGTGGAATTTGCGGATAGTTTTAACTTCAATCCTCACAAATGGTTGCTGGTAAACTTCGACTGTAGTGCGATGTGGGTCAAGAAAAGGACCGACCTAACCGGCGCATTCAGATTAGATCCAACGTATCTGAAGCATTCCCACCAGGATAGTGGCCTTATAACAGACTATAGGCACTGGCAGATCCCGTTAGGTAGGCGTTTTAGGAGTCTAAAGATGTGGTTTGTGTTTCGTATGTATGGGGTAAAGGGGCTGCAAGCGTATATAAGAAAACATGTCCAGCTTTCACACGAGTTCGAATCCTTGGTTAGACAAGACCCTAGATTCGAAATTTGTGTTGAGGTGATTTTGGGGCTAGTTTGTTTTAGACTAAAAGGTTCCAACAAGGTTAATGAAGCGCTGCTTCAGAGGATAAACAGCGCCAAGAAAATTCATTTGGTTCCCTGCCATTTGCGTGACAAGTTCGTTTTGAGGTTCGCGATATGCTCACGTACAGTAGAATCAGCGCATGTACAGAGAGCCTGGGAGCATATTAAGGAATTGGCGGCGGATGTTTTGCGTGCGGAACGTGAGTGA

Part BBa_K2672002: DBH

This basic part is the budding yeast codon-optimized gene that encodes the human Dopamine beta-hydroxylase: EC1.14.17.1. This enzyme catalyzes the addition reaction of an alcohol group on the dopamine molecule to form noradrenaline. This reaction also requires an ascorbate and a dioxygen molecule as a reducer and an oxygen donor respectively. The enzyme uses copper cations as cofactors. This is the third step of the biosynthesis of adrenaline.

The crystallographic structure is already available on the Uniprot database: P09172. The protein is a homotetramer made of two disulfide-linked dimers.

ATGCCGGCCCTTAGCCGTTGGGCCAGCCTACCTGGGCCGTCAATGCGTGAGGCCGCGTTTATGTATTCTACAGCGGTGGCCATCTTTTTGGTGATACTGGTAGCCGCGCTTCAAGGATCAGCCCCACGTGAAAGCCCTTTGCCATATCATATTCCCCTAGATCCTGAAGGCTCACTTGAGTTGTCTTGGAACGTCAGCTACACTCAAGAGGCTATCCATTTTCAGTTATTGGTTAGGAGGCTGAAGGCGGGTGTGTTATTCGGCATGTCCGATAGAGGAGAATTAGAAAACGCTGACCTGGTCGTGCTATGGACGGATGGTGACACCGCTTATTTCGCGGATGCTTGGTCAGATCAGAAAGGTCAAATCCATCTTGACCCCCAGCAAGATTACCAACTACTACAGGTTCAAAGGACACCGGAAGGGCTGACATTACTATTTAAGAGGCCGTTTGGTACATGTGACCCAAAAGATTACCTGATCGAAGACGGCACAGTTCATCTAGTATACGGTATCCTGGAAGAGCCATTCAGGAGTTTGGAGGCCATAAATGGTTCCGGGTTGCAGATGGGGCTTCAGAGGGTTCAGTTGTTAAAACCAAATATCCCTGAACCGGAATTACCATCCGACGCATGCACGATGGAAGTTCAGGCCCCTAACATTCAAATCCCCAGCCAAGAGACAACGTATTGGTGTTATATAAAGGAGTTACCGAAAGGCTTTTCCAGGCACCATATAATCAAATATGAACCGATAGTGACAAAGGGAAATGAGGCCTTAGTACACCATATGGAGGTTTTTCAATGCGCCCCCGAGATGGACTCCGTGCCCCACTTTTCCGGCCCATGTGACTCAAAAATGAAGCCCGATAGGCTTAATTATTGCAGGCATGTTTTGGCAGCTTGGGCCCTAGGAGCGAAGGCGTTCTATTACCCTGAAGAGGCGGGACTTGCATTTGGAGGCCCTGGCTCATCACGTTACCTGAGATTGGAAGTACACTACCACAACCCCCTAGTAATTGAGGGCCGTAACGACTCTTCCGGCATTAGGCTTTATTACACCGCGAAGTTGAGAAGATTCAATGCCGGGATCATGGAGCTAGGACTCGTTTACACTCCGGTGATGGCGATACCACCTAGAGAAACGGCCTTCATACTAACGGGTTATTGCACCGATAAATGCACGCAACTGGCGCTGCCGCCCTCTGGTATTCATATATTTGCGAGCCAGTTACATACGCATTTGACAGGGCGTAAGGTTGTTACAGTTCTTGTCCGTGACGGGAGAGAATGGGAAATTGTCAATCAAGACAACCATTATTCTCCGCATTTTCAAGAGATACGTATGTTAAAAAAGGTCGTAAGCGTCCACCCTGGGGACGTCCTAATCACCAGTTGCACGTATAACACGGAGGATAGGGAGTTGGCTACTGTGGGTGGGTTTGGTATCCTGGAAGAAATGTGTGTAAACTATGTCCACTACTACCCCCAAACCCAGCTAGAGTTGTGTAAGAGTGCGGTTGACGCCGGGTTTTTGCAAAAATATTTTCACCTGATAAACCGTTTCAACAATGAGGATGTATGTACGTGTCCGCAGGCTAGTGTTTCTCAACAATTTACAAGCGTTCCGTGGAACTCTTTTAACAGAGATGTTTTAAAAGCGCTTTATTCATTCGCTCCCATTTCTATGCATTGCAACAAGAGTAGTGCAGTCAGGTTCCAAGGCGAGTGGAATCTACAGCCGTTGCCGAAGGTCATATCAACATTGGAAGAGCCAACGCCTCAATGCCCTACCAGTCAGGGTAGGAGCCCGGCGGGCCCCACAGTCGTGTCAATTGGAGGCGGCAAAGGTTGA

Part BBa_K267003: PNMT

This basic part is the budding yeast codon-optimized gene that code for the human Phenylethanolamine N-methyltransferase (PNMT): EC2.1.1.28. The PNMT enzyme catalyzes the biochemical reaction of the transformation of noradrenaline into adrenaline. This reaction also requires S-adenosyl-L-methionine as a methyl group giver. This is the fourth and final step of the biosynthesis of adrenaline.

The crystallographic structure is already available on the Uniprot database: P11086.

ATGTCAGGAGCGGACAGAAGTCCAAATGCGGGAGCTGCTCCTGATAGCGCGCCAGGTCAAGCGGCTGTTGCAAGTGCATATCAACGTTTCGAGCCAAGAGCATACTTGAGGAACAACTATGCACCGCCCAGGGGAGACCTGTGCAACCCGAACGGGGTCGGTCCATGGAAACTGAGATGTTTAGCCCAAACGTTTGCTACTGGGGAGGTTTCAGGGAGGACTCTGATTGATATAGGGAGTGGACCTACAGTTTACCAGCTTCTTTCAGCCTGTAGTCACTTTGAGGACATCACGATGACTGACTTTCTTGAGGTAAACAGACAAGAACTGGGCAGGTGGCTACAGGAGGAACCAGGTGCATTTAATTGGTCAATGTACTCACAACATGCTTGTCTAATTGAGGGGAAAGGGGAATGCTGGCAGGATAAGGAACGTCAACTTAGAGCTAGAGTAAAGCGTGTGCTTCCCATTGATGTGCACCAGCCGCAACCACTAGGTGCAGGTAGTCCCGCGCCGCTTCCTGCGGATGCGTTAGTCTCCGCGTTTTGTCTGGAGGCGGTGTCACCGGATTTGGCCTCCTTCCAGCGTGCGCTAGACCACATTACCACACTTTTACGTCCGGGAGGTCACCTTCTGCTGATAGGGGCCCTTGAGGAATCCTGGTATTTGGCAGGCGAAGCACGTCTAACTGTTGTCCCCGTCTCCGAAGAGGAGGTACGTGAAGCCTTAGTCAGGTCTGGCTATAAGGTCAGAGATTTGAGAACGTACATAATGCCAGCGCACCTCCAGACGGGAGTCGATGACGTGAAGGGGGTTTTCTTCGCCTGGGCGCAGAAGGTCGGGTTG

References

1. Burkhard, P. et al., 2001. Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Nature Structural and Molecular Biology, Volume 8, p. 963–967.