1999
DOI: 10.1016/s1389-1723(00)80017-1
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Purification and characterization of N-Acetylglucosamine 6-phosphate deacetylase from Thermus caldophilus

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Cited by 4 publications
(1 citation statement)
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“…16 The enzymes from different organisms show variable oligomeric organization. As in E. coli, the NAGPases purified from the bacteria Thermus caldophilus, 17 V. cholerae, 18 and Alteromonas sp. 19 are tetrameric proteins, in contrast with B. subtilis deacetylase that has been shown to be a dimer.…”
Section: Introductionmentioning
confidence: 99%
“…16 The enzymes from different organisms show variable oligomeric organization. As in E. coli, the NAGPases purified from the bacteria Thermus caldophilus, 17 V. cholerae, 18 and Alteromonas sp. 19 are tetrameric proteins, in contrast with B. subtilis deacetylase that has been shown to be a dimer.…”
Section: Introductionmentioning
confidence: 99%