Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536
Aims: The key enzyme in the fructose‐6‐phosphate shunt in bifidobacteria, Fructose‐6‐phosphate phosphoketolase (F6PPK; E.C. 4.1.2.22.), was purified to electrophoretic homogeneity for the first time from Bifidobacterium longum (BB536). Methods and Results: A three‐step procedure comprising aceton...
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| Format: | Article |
| Language: | English |
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Oxford University Press
2001
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| Online Access: | http://psasir.upm.edu.my/id/eprint/111879/ http://psasir.upm.edu.my/id/eprint/111879/3/111879.pdf |
| _version_ | 1848865803523325952 |
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| author | Fandi, K.G. Ghazali, H.M. Yazid, A.M. A.R., Raha |
| author_facet | Fandi, K.G. Ghazali, H.M. Yazid, A.M. A.R., Raha |
| author_sort | Fandi, K.G. |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Aims: The key enzyme in the fructose‐6‐phosphate shunt in bifidobacteria, Fructose‐6‐phosphate phosphoketolase (F6PPK; E.C. 4.1.2.22.), was purified to electrophoretic homogeneity for the first time from Bifidobacterium longum (BB536).
Methods and Results: A three‐step procedure comprising acetone fractionation followed by fast protein liquid chromatography (FPLC) resulted in a 30‐fold purification. The purified enzyme had a molecular mass of 300 ± 5 kDa as determined by gel filtration. It is probably a tetramer containing two different subunits with molecular masses of 93 ± 1 kDa and 59 ± 0.5 kDa, as determined by SDS‐PAGE.
Conclusions: The deduced N‐terminal amino acid sequences of the two subunits revealed no significant similarity between them and other proteins when compared to the data bases of EMBL and SWISS‐PROT, indicating that this could be the first report on N‐terminal amino acid sequence of F6PPK.
Significance and Impact of the Study: The data from this study will be used to design oligonucleotide probe specific for bifidobacteria and to study the gene encoded F6PPK. |
| first_indexed | 2025-11-15T14:10:31Z |
| format | Article |
| id | upm-111879 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T14:10:31Z |
| publishDate | 2001 |
| publisher | Oxford University Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1118792025-03-12T03:55:52Z http://psasir.upm.edu.my/id/eprint/111879/ Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 Fandi, K.G. Ghazali, H.M. Yazid, A.M. A.R., Raha Aims: The key enzyme in the fructose‐6‐phosphate shunt in bifidobacteria, Fructose‐6‐phosphate phosphoketolase (F6PPK; E.C. 4.1.2.22.), was purified to electrophoretic homogeneity for the first time from Bifidobacterium longum (BB536). Methods and Results: A three‐step procedure comprising acetone fractionation followed by fast protein liquid chromatography (FPLC) resulted in a 30‐fold purification. The purified enzyme had a molecular mass of 300 ± 5 kDa as determined by gel filtration. It is probably a tetramer containing two different subunits with molecular masses of 93 ± 1 kDa and 59 ± 0.5 kDa, as determined by SDS‐PAGE. Conclusions: The deduced N‐terminal amino acid sequences of the two subunits revealed no significant similarity between them and other proteins when compared to the data bases of EMBL and SWISS‐PROT, indicating that this could be the first report on N‐terminal amino acid sequence of F6PPK. Significance and Impact of the Study: The data from this study will be used to design oligonucleotide probe specific for bifidobacteria and to study the gene encoded F6PPK. Oxford University Press 2001 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/111879/3/111879.pdf Fandi, K.G. and Ghazali, H.M. and Yazid, A.M. and A.R., Raha (2001) Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536. Letters in Applied Microbiology, 32 (4). pp. 235-239. ISSN 0266-8254; eISSN: 1472-765X https://academic.oup.com/lambio/article-abstract/32/4/235/6704215?redirectedFrom=fulltext 10.1046/j.1472-765x.2001.00895.x |
| spellingShingle | Fandi, K.G. Ghazali, H.M. Yazid, A.M. A.R., Raha Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 |
| title | Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 |
| title_full | Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 |
| title_fullStr | Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 |
| title_full_unstemmed | Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 |
| title_short | Purification and N‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from Bifidobacterium longum BB536 |
| title_sort | purification and n‐terminal amino acid sequence of fructose‐6‐phosphate phosphoketolase from bifidobacterium longum bb536 |
| url | http://psasir.upm.edu.my/id/eprint/111879/ http://psasir.upm.edu.my/id/eprint/111879/ http://psasir.upm.edu.my/id/eprint/111879/ http://psasir.upm.edu.my/id/eprint/111879/3/111879.pdf |