Literature summary for 1.2.5.2 extracted from

Xu, S.; Minteer, S.
Investigating the impact of multi-heme pyrroloquinoline quinone-aldehyde dehydrogenase orientation on direct bioelectrocatalysis via site specific enzyme immobilization (2013), ACS Catal., 3, 1756-1763.

No PubMed abstract available

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Application

Application	Comment	Organism
synthesis	application in direct bioelectrocatalysis via site specific immobilization to form a monolayer of biocatalysts with a uniform orientation toward the gold electrode. Six-histidine tags at the N- or C-terminus of each of the three subunits are utilized as linking sites to performsite specific immobilization. The orientation of multi-subunit enzymes can affect direct electron transfer greatly by varying the electron tunneling distances. The favorable orientation allowing for a minimal heme c electron transfer distance shows a direct electron transfer rate 6.6fold higher than that with the orientation closest to the active site of the enzyme	Gluconobacter oxydans

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Gluconobacter sp. DSM 3504	Gluconobacter oxydans

Organism

Organism	UniProt	Comment	Textmining
Gluconobacter oxydans	-	-	-
Gluconobacter oxydans DSM 3504	-	-	-

Synonyms

Synonyms	Comment	Organism
PQQ-AlDH	-	Gluconobacter oxydans
pyrroloquinoline quinone-dependent aldehyde dehydrogenase	-	Gluconobacter oxydans

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Release 2023.1 (January 2023)