Literature summary for 4.4.1.30 extracted from

Gasper, R.; Schwach, J.; Hartmann, J.; Holtkamp, A.; Wiethaus, J.; Riedel, N.; Hofmann, E.; Frankenberg-Dinkel, N.
Distinct features of cyanophage-encoded T-type phycobiliprotein lyase PhiCpeT The role of auxiliary metabolic genes (2017), J. Biol. Chem., 292, 3089-3098 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.8 A resolution	Prochlorococcus phage P-HM1

Organism

Organism	UniProt	Comment	Textmining
Prochlorococcus phage P-HM1	E3SMK9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme specifically binds bilins with a reduced 15,16-double bond. The complex with phycoerythrobilin is highly stable and displays a strong red fluorescence. CpeT does not transfer phycoerythrobilin to the host phycobiliprotein beta-subunit but is able to assist the host layse	Prochlorococcus phage P-HM1	?	-	?

Synonyms

Synonyms	Comment	Organism
CpeT	-	Prochlorococcus phage P-HM1
PhiCpeT	-	Prochlorococcus phage P-HM1

General Information

General Information	Comment	Organism
physiological function	enzyme specifically binds phycoerythrobilin in vitro leading to a tight complex. The complex is not directly able to transfer phycoerythrobilin to the host phycobiliprotein beta-subunit. However, it can assist the host lyase CpeS in its function	Prochlorococcus phage P-HM1

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Release 2023.1 (January 2023)