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PMID:15262231
| Citation |
Richards, GP, Hammer, CH, Garfield, MK and Parveen, S (2004) Characterization of a lysyl aminopeptidase activity associated with phosphoglucose isomerase of Vibrio vulnificus. Biochim. Biophys. Acta 1700:219-29 |
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| Abstract |
Phosphoglucose isomerase (PGI) is a multifunctional enzyme involved in glycolysis and gluconeogenesis and, in mammalian cells, functions as neuroleukin, autocrine motility factor (AMF), and differentiation and maturation factor (MF). We isolated and characterized PGI with a novel lysyl aminopeptidase (LysAP) activity (PGI-LysAP) from Vibrio vulnificus. Mass spectrometry revealed that PGI-LysAP is a heterodimer consisting of 23.4- and 60.8-kDa subunits. Only the heterodimer displayed LysAP activity. PGI-LysAP has a pI around 6.0 and high specificity toward the synthetic, fluorogenic substrate l-lysyl-7-amino-4-methylcoumarin. LysAP activity is optimal at pH 8.0, is 64% higher at 37 degrees C than at 21 degrees C, does not directly correlate with virulence, and is strongly inhibited by serine protease and metalloprotease inhibitors. PGI-LysAP was also identified in Vibrio parahaemolyticus and V. cholerae, but was absent from non-Vibrio human pathogens. Sequencing of the pgi gene revealed 1653 bp coding for a 550-amino-acid protein. Cloned and expressed PGI formed a homodimer with isomerase activity, but not LysAP activity. The finding of LysAP activity associated with heterodimeric PGI should foster a broad search for putative substrates in an effort to elucidate the role of PGI-LysAP in bacteria and its roles in the pathophysiology of diseases. |
| Links |
PubMed Online version:10.1016/j.bbapap.2004.05.005 |
| Keywords |
Amino Acid Sequence; Aminopeptidases/metabolism; Bacterial Proteins; Enzyme Inhibitors; Glucose-6-Phosphate Isomerase/chemistry; Glucose-6-Phosphate Isomerase/isolation & purification; Glucose-6-Phosphate Isomerase/metabolism; Molecular Sequence Data; Protein Structure, Quaternary; Protein Subunits; Substrate Specificity; Vibrio vulnificus/enzymology; Vibrio vulnificus/pathogenicity |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004347: glucose-6-phosphate isomerase activity |
ECO:0000314: |
F |
Figure 3b: Isomerase activity was readily detectable in PGI-LysAP from V. vulnificus. Assay of commercially available PGI from rabbit, B. stearothermophilus, and S. cerevisiae also revealed isomerase activity. Determination of the pH optima for isomerase activity for PGI from V. vulnificus. |
complete | ||||
|
enables |
GO:0004347: glucose-6-phosphate isomerase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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