Literature summary for 3.1.1.76 extracted from

Hisano, T.; Tezuka, Y.; Kasuya, K.; Kbayashi, T.; Shiraki, M.; Iwata, T.; Doi, Y.; Saito, T.; Miki, K.
Crystal structure of the type II PHA depolymerase (2005), Polym. Reprints, 46, 253-254.

No PubMed abstract available

Search for more literature for 3.1.1.76

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure determination and analysis at 1.7 A resolution	Talaromyces funiculosus

Organism

Organism	UniProt	Comment	Textmining
Talaromyces funiculosus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
[oxycarbonyl[(R)-2-pentylethylene]]n + H2O = [oxycarbonyl[(R)-2-pentylethylene]]m + [oxycarbonyl[(R)-2-pentylethylene]]g	active site residues are Ser19, Asp101, and His135 located at the bottom of a crevice, two possible PHA degradation reaction mechanisms	Talaromyces funiculosus	a

Subunits

Subunits	Comment	Organism
More	the enzyme shows a alpha/beta hydrolase fold with a topological arrangement resulting from circular permutation	Talaromyces funiculosus

Synonyms

Synonyms	Comment	Organism
PHA depolymerase	-	Talaromyces funiculosus
polyhydroxyalkanoate depolymerase	-	Talaromyces funiculosus
type II PHA depolymerase	-	Talaromyces funiculosus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)