tulge-tcab1

Tulipa gesneriana (Garden tulip). Tuliposide A-converting enzyme b1, amyloplastic

Comment

(from uniprot) Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B. 6-tuliposide A and tuliposide A-converting enzyme, which are compartmentalized in the vacuoles and plastids respectively, come into contact with each other for the enzyme reaction releasing toxic tulipalin A upon cell disruption by pathogen infection or herbivore predation

Relationship

Family : Plant_carboxylesterase

Block : H

Position in NCBI Life Tree : Tulipa gesneriana

Molecular evidence

No mutation

No structure

No kinetic

No disease

No inhibitor

Database

Sequence

Peptide

MSVALFCGPP PAVSFGCKDG RGRKGMVRSK DIVRQTVKPP AHACRLIGWN KYPGSVVPTN SSLSPSPTAL DDEIELDLSP FLIIYKDGRI ERLKGTTVIP ACPEVATKDV IIDPATGVSV RLYLPNVVDL PSKKLPVLVY FHGGGFVIEN TGSPNYHNYL TLLAAKSGLL IVSVNYRLAP EHPIPASFDD CMAGFNWVVS HSAGPAPEPW LARHGDLTQI LISGDSAGGT VTHYVLLRAD AGVIEGAALV HPYFLGSKRL ENQTEEDFEF HEKLWRLSTP DTEGLDDPLI NPLAPGAPSL AGLKCKRAVV FVAELDFLVE RGRMYYDALV KSGWGGKAEL VHQEGVGHVF HLSDYSGDVS VDMMAKMVAF LRGE

References

Title : Molecular diversity of tuliposide A-converting enzyme in the tulip - Nomura_2013_Biosci.Biotechnol.Biochem_77_1042
Author(s) : Nomura T , Tsuchigami A , Ogita S , Kato Y
Ref : Biosci Biotechnol Biochem , 77 :1042 , 2013
Abstract : Nomura_2013_Biosci.Biotechnol.Biochem_77_1042
ESTHER : Nomura_2013_Biosci.Biotechnol.Biochem_77_1042
PubMedSearch : Nomura_2013_Biosci.Biotechnol.Biochem_77_1042
PubMedID: 23649245
Gene_locus related to this paper: tulge-tcab2 , tulge-tcab1 , tulge-tcab3 , tulge-tcab4