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• W2055369599 endingPage "2258" @default.
• W2055369599 startingPage "2252" @default.
• W2055369599 abstract "ABSTRACT The pgmG gene of Sphingomonas paucimobilis ATCC 31461, the industrial gellan gum-producing strain, was cloned and sequenced. It encodes a 50,059-Da polypeptide that has phosphoglucomutase (PGM) and phosphomannomutase (PMM) activities and is 37 to 59% identical to other bifunctional proteins with PGM and PMM activities from gram-negative species, including Pseudomonas aeruginosa AlgC. Purified PgmG protein showed a marked preference for glucose-1-phosphate (G1P); the catalytic efficiency was about 50-fold higher for G1P than it was for mannose-1-phosphate (M1P). The estimated apparent K m values for G1P and M1P were high, 0.33 and 1.27 mM, respectively. The pgmG gene allowed the recovery of alginate biosynthetic ability in a P. aeruginosa mutant with a defective algC gene. This result indicates that PgmG protein can convert mannose-6-phosphate into M1P in the initial steps of alginate biosynthesis and, together with other results, suggests that PgmG may convert glucose-6-phosphate into G1P in the gellan pathway." @default.
• W2055369599 created "2016-06-24" @default.
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• W2055369599 date "2000-05-01" @default.
• W2055369599 modified "2023-10-05" @default.
• W2055369599 title "Identification of the <i>pgmG</i> Gene, Encoding a Bifunctional Protein with Phosphoglucomutase and Phosphomannomutase Activities, in the Gellan Gum-Producing Strain <i>Sphingomonas paucimobilis</i> ATCC 31461" @default.
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• W2055369599 doi "https://doi.org/10.1128/aem.66.5.2252-2258.2000" @default.
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