Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
ThrH, a homoserine kinase isozyme with in vivo phosphoserine phosphatase activity in Pseudomonas aeruginosa.
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Native P. aeruginosa double-mutant evidence establishes that ThrH can substitute for ThrB in threonine synthesis. The historical kinase label does not establish ATP-dependent chemistry; the later biochemical study resolves the donor.
"In P.
aeruginosa, threonine auxotrophy is observed only when both thrB and thrH are
simultaneously inactivated."
The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity.
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HPLC assays establish phosphoserine-dependent phosphorylation of homoserine, distinct from ATP-dependent homoserine kinase. The parallel phosphoserine hydrolysis assay supports a second demonstrated catalytic activity.
"ThrH is able to further transfer the phosphoryl group to
homoserine using phosphoserine as the phosphoryl group donor"
Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction.
p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase.
UniProt record for PSEAE thrH