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Literature summary for 3.1.1.75 extracted from

  • Trainer, M.A.; Capstick, D.; Zachertowska, A.; Lam, K.N.; Clark, S.R.; Charles, T.C.
    Identification and characterization of the intracellular poly-3-hydroxybutyrate depolymerase enzyme PhaZ of Sinorhizobium meliloti (2010), BMC Microbiol., 10, 92.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Sinorhizobium meliloti

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
Sinorhizobium meliloti 5622
-

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly-3-hydroxybutyrate + H2O
-
Sinorhizobium meliloti ?
-
?

Synonyms

Synonyms Comment Organism
PhaZ
-
Sinorhizobium meliloti
poly(3-hydroxybutyrate) depolymerase
-
Sinorhizobium meliloti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Sinorhizobium meliloti

General Information

General Information Comment Organism
malfunction a phaZ mutant exhibits increased poly-3-hydroxybutyrate accumulation during free-living growth, even when grown under non-poly-3-hydroxybutyrate -inducing conditions. The phaZ mutant demonstrates no reduction in symbiotic capacity. This mutant also exhibits a decreased capacity to tolerate long-term carbon starvation, comparable to that of other poly-3-hydroxybutyrate cycle mutants. In contrast to other poly-3-hydroxybutyrate cycle mutants, the phaZ mutant does not exhibit any decrease in rhizosphere competitiveness, but it exhibits a significant increase in succinoglycan biosynthesis Sinorhizobium meliloti