Literature summary for 4.2.2.2 extracted from

McDonough, M.A.; Ryttersgaard, C.; Bjornvad, M.E.; Lo Leggio, L.; Schulein, M.; Schroder Glad, S.O.; Larsen, S.
Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima (2002), Acta Crystallogr. Sect. D, 58, 709-711.

Search for more literature for 4.2.2.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Bacillus licheniformis	Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of mutant enzyme C132I/C156N/C194L, hanging-drop vapour-diffusion method	Thermotoga maritima

Protein Variants

Protein Variants	Comment	Organism
C132I/C156N/C194L	mutations increase expression level	Thermotoga maritima

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Thermotoga maritima	the enzyme is involved in degradation of the pectate portion of the primary plant cell wall	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9WYR4	DSM 3109	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is involved in degradation of the pectate portion of the primary plant cell wall	Thermotoga maritima	?	-	?

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Release 2023.1 (January 2023)