Phenotypic Assay on L - Sorbose

نویسندگان

  • Lulu Huang
  • Lou Massa
  • Jerome Karle
  • Ian S. Millett
  • Jaby Jacob
  • Bojan Zagrovic
  • Thomas M. Dillon
  • Nikolina Cingel
  • Robin S. Dothager
  • Soenke Seifert
  • P. Thiyagarajan
  • Tobin R. Sosnick
  • M. Zahid Hasan
  • Vijay S. Pande
  • Ingo Ruczinski
  • Sebastian Doniach
  • Aaron E. Hirsh
چکیده

BIOCHEMISTRY. For the article ‘‘Kernel energy method: Application to insulin,’’ by Lulu Huang, Lou Massa, and Jerome Karle, which appeared in issue 36, September 6, 2005, of Proc. Natl. Acad. Sci. USA (102, 12690–12693; first published August 24, 2005; 10.1073 pnas.0506378102), the authors note an error in a funding acknowledgment: ‘‘L.M. thanks the National Institutes of Health for National Institute of General Medical Sciences Grant MBRS SCORE5 S06GM606654 and National Center For Research Resources Grant RR-0307 and the National Science Foundation for Centers of Research Excellence in Science and Technology grant support’’ should read: ‘‘L.M. thanks the National Institutes of Health for National Institute of General Medical Sciences Grant MBRS SCORE5 S06GM606654 and the National Science Foundation for Centers of Research Excellence in Science and Technology grant support. This investigation was supported by Research Centers in Minority Institutions’ Award RR-03037 from the National Center for Research Resources, National Institutes of Health.’’

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Taxonomic characterization of Ketogulonigenium vulgare gen. nov., sp. nov. and Ketogulonigenium robustum sp. nov., which oxidize L-sorbose to 2-keto-L-gulonic acid.

Four bacterial strains that oxidize L-sorbose to 2-keto-L-gulonic acid, a key intermediate in the synthesis of vitamin C, were isolated from soils of geographically distinct locations. All were Gram-negative, facultatively anaerobic, chemoheterotrophic rods. Comparative analysis revealed nearly identical 16S rDNA sequences amongst them (99.7-100% identical) and identified them as members of the...

متن کامل

NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Gluconobacter suboxydans IFO 3291.

The NADPH-dependent L-sorbose reductase (SR) of L-sorbose-producing Gluconobacter suboxydans IFO 3291 contributes to intracellular L-sorbose assimilation. The gene disruptant showed no SR activity and did not assimilate the once-produced L-sorbose, indicating that the SR functions mainly as an L-sorbose-reducing enzyme in vivo and not as a D-sorbitol-oxidizing enzyme.

متن کامل

Pathway of L-sorbose metabolism in Aerobacter aerogenes.

The pathway of L-sorbose metabolism in Aerobacter aerogenes was determined to be: L-sorbose ---f L-sorbose l-phosphate ---f D-glucitol 6-phosphate -+ D-fructose 6-phosphate. Phosphorylation of L-sorbose at C-l is mediated by a phosphoenolpyruvate-dependent phosphotransferase system, whereas r,-sorbose l-phosphate reduction and D-glucitol 6-phosphate oxidation are mediated by pyridine-nucleotide...

متن کامل

L-sorbose reductase and its transcriptional regulator involved in L-sorbose utilization of Gluconobacter frateurii.

Upstream of the gene for flavin adenine dinucleotide (FAD)-dependent D-sorbitol dehydrogenase (SLDH), sldSLC, a putative transcriptional regulator was found in Gluconobacter frateurii THD32 (NBRC 101656). In this study, the whole sboR gene and the adjacent gene, sboA, were cloned and analyzed. sboR mutation did not affect FAD-SLDH activity in the membrane fractions. The SboA enzyme expressed an...

متن کامل

Genetics of L-sorbose transport and metabolism in Lactobacillus casei.

Genes encoding L-sorbose metabolism of Lactobacillus casei ATCC 393 have been identified on a 6.8-kb chromosomal DNA fragment. Sequence analysis revealed seven complete genes and a partial open reading frame transcribed as two units. The deduced amino acid sequences of the first transcriptional unit (sorRE) showed high similarity to the transcriptional regulator and the L-sorbose-1-phosphate re...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005