Coelenterazine sulfotransferase from Renilla muelleri

G Tzertzinis, B Baker, J Benner, E Brown, IR Corrêa Jr… - Plos one, 2022 - journals.plos.org
The luciferin sulfokinase (coelenterazine sulfotransferase) of Renilla was previously
reported to activate the storage form, luciferyl sulfate (coelenterazine sulfate) to luciferin …

Sulfoluciferin is biosynthesized by a specialized luciferin sulfotransferase in fireflies

TR Fallon, FS Li, MA Vicent, JK Weng - Biochemistry, 2016 - ACS Publications
Firefly luciferin is a specialized metabolite restricted to fireflies (family Lampyridae) and other
select families of beetles (order Coleoptera). Firefly luciferin undergoes luciferase-catalyzed …

Enzymatic sulfation of coelenterazine by human cytosolic aryl sulfotransferase SULT1A1: identification of coelenterazine C2-benzyl monosulfate by LC/ESI-TOF-MS

S Inouye, K Matsuda, M Nakamura - Biochemical and Biophysical …, 2023 - Elsevier
Coelenterazine (CTZ) is known as a light-emitting source for the bioluminescence reaction
in marine organisms. CTZ has two phenolic hydroxy groups at the C2-benzyl and C6-phenyl …

Similar enzymatic functions in distinct bioluminescence systems: evolutionary recruitment of sulfotransferases in ostracod light organs

ES Lau, JA Goodheart, NT Anderson… - Biology …, 2024 - royalsocietypublishing.org
Genes from ancient families are sometimes involved in the convergent evolutionary origins
of similar traits, even across vast phylogenetic distances. Sulfotransferases are an ancient …

A factor-dependent sulfotransferase specific for 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in the Cyanobacterium Synechococcus 6301

A Schmidt, U Christen - Planta, 1978 - Springer
A sulfotransferase isolated from the Cyanobacterium Synechococcus 6301 was found to be
specific for 3′-phosphoadenosine-5′-phosphosulfate (PAPS). The molecular weight of …

Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase

MS Titushin, SV Markova, LA Frank… - Photochemical & …, 2008 - Springer
The Renilla bioluminescent system in vivo is comprised of three proteins—the luciferase,
green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called …

Structure–function studies on the active site of the coelenterazine‐dependent luciferase from Renilla

J Woo, MH Howell, AG Von Arnim - Protein Science, 2008 - Wiley Online Library
Renilla luciferase (RLUC) is a versatile tool for gene expression assays and in vivo
biosensor applications, but its catalytic mechanism remains to be elucidated. RLUC is …

Partial Purification and Characterization of a 3′- Phosphoadenosine 5′ -Phosphosulfate: Desulfoglucosinolate Sulfotransferase from Cress (Lepidium sativum)

TM Glendening, JE Poulton - Plant Physiology, 1990 - academic.oup.com
Abstract A 3′-phosphoadenosine 5′-phosphosulfate (PAPS): desulfoglucosinolate
sulfotransferase (EC 2.8. 2-) was extensively purified from light-grown cress (Lepidium …

Expression, purification and luminescence properties of coelenterazine-utilizing luciferases from Renilla, Oplophorus and Gaussia: comparison of substrate specificity …

S Inouye, Y Sahara-Miura, J Sato, R Iimori… - Protein Expression and …, 2013 - Elsevier
The cold-induced expression system in Escherichia coli is useful and we have applied this
system to prepare the coelenterazine-utilizing luciferases including Renilla luciferase …

Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis

AM Loening, TD Fenn, SS Gambhir - Journal of molecular biology, 2007 - Elsevier
Due to its ability to emit light, the luciferase from Renilla reniformis (RLuc) is widely
employed in molecular biology as a reporter gene in cell culture experiments and small …