Literature summary for 4.2.2.26 extracted from

Kim, H.S.; Chu, Y.J.; Park, C.-H.; Lee, E.Y.; Kim, H.S.
Site-directed mutagenesis-based functional analysis and characterization of endolytic lyase activity of N- and C-terminal domains of a novel oligoalginate lyase from Sphingomonas sp. MJ-3 possessing exolytic lyase activity in the intact enzyme (2015), Mar. Biotechnol., 17, 782-792.

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Protein Variants

Protein Variants	Comment	Organism
H178A	mutant shows reduced oligoalginate lyase activity	Sphingomonas sp.
H389A	mutant shows reduced oligoalginate lyase activity	Sphingomonas sp.
N177A	mutant shows reduced oligoalginate lyase activity	Sphingomonas sp.
R236A	mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity	Sphingomonas sp.
Y234F	mutant shows reduced oligoalginate lyase activity	Sphingomonas sp.
Y426F	mutant shows reduced oligoalginate lyase activity	Sphingomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Sphingomonas sp.	G1EH67	-	-
Sphingomonas sp. MJ-3	G1EH67	-	-

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Release 2023.1 (January 2023)