2.4.1.B34: 4,6-alpha-glucanotransferase
This is an abbreviated version!
For detailed information about 4,6-alpha-glucanotransferase, go to the full flat file.
Reaction
The enzyme uses maltooligosaccharides as donor and acceptor substrates. It cleaves alpha1->4 glucosidic bonds and synthesizes 1->6 and 1->4 glucosidic linkages. =
Synonyms
4, 6-alpha-glucanotransferase, 4,6-alpha-GT, 4,6-alpha-GTase, Achr_35950, Exig_2648, GflML4, Gtf106b, GtfB, GTFB protein, GTFB-like 4,6-alpha-glucanotransferase, GtfB-like 4,6-alpha-glucanotransferases, GTFB-like 4,6-alpha-GT, GTFC, GTFC-like 4,6-alpha-glucanotransferase, GTFC-like 4,6-alpha-GT, GtfD, GtfML4, GtfW, GtfX, GtfY, Lreu_1346, UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein
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Engineering
Engineering on EC 2.4.1.B34 - 4,6-alpha-glucanotransferase
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D1015N
additional information
mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose)
D1015N
mutation in putative nucleophile, mutant shows no activity on maltooligosaccharides
D1015N
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mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose)
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construction of deletion mutant GtfX-DELTANDELTAC encoding residues 448-1304, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
additional information
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construction of deletion mutant GtfY-DELTANDELTAC encoding residues 438-1290, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
additional information
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construction of deletion mutant GtfX-DELTANDELTAC encoding residues 448-1304, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
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additional information
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construction of deletion mutant GtfY-DELTANDELTAC encoding residues 438-1290, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
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additional information
removal of the variable N-terminal region of the GTFB enzyme (yielding construct GTFB734-1619) results in increased expression of soluble and active enzyme in Escherichia coli
additional information
an (engineered) 4,6-alpha-glucanotransferase (GTFB) from Lactobacillus reuteri 121 is introduced into two potato genetic backgrounds: amylose-containing line Kardal and amylose-free mutant amf. The resulting starches show severe changes in granule morphology regardless of genetic backgrounds. Modified starches from amf background exhibit a significant increase in granule size and starch phosphate content relative to the control, while starches from Kardal background display a higher digestibility, but do not show changes in granule size and phosphate content. Transcriptome analysis reveal the existence of a mechanism to restore the regular packing of double helices in starch granules, which possibly results in the removal of novel glucose chains potentially introduced by the (engineered) GTFB. This amendment mechanics can also explain the difficulties to detect alterations in starch fine structure in the transgenic lines
additional information
construction of deletion GtfB-DELTANDELTAV mutant D1015N
additional information
construction of the GtfB-DELTAN-DELTAV mutant, a truncated variant (amino acids 761 to 1619) of GtfB of Lactobacillus reuteri strain 121 lacking both the N-terminal variable domain and domain V
additional information
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construction of the GtfB-DELTAN-DELTAV mutant, a truncated variant (amino acids 761 to 1619) of GtfB of Lactobacillus reuteri strain 121 lacking both the N-terminal variable domain and domain V
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additional information
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an (engineered) 4,6-alpha-glucanotransferase (GTFB) from Lactobacillus reuteri 121 is introduced into two potato genetic backgrounds: amylose-containing line Kardal and amylose-free mutant amf. The resulting starches show severe changes in granule morphology regardless of genetic backgrounds. Modified starches from amf background exhibit a significant increase in granule size and starch phosphate content relative to the control, while starches from Kardal background display a higher digestibility, but do not show changes in granule size and phosphate content. Transcriptome analysis reveal the existence of a mechanism to restore the regular packing of double helices in starch granules, which possibly results in the removal of novel glucose chains potentially introduced by the (engineered) GTFB. This amendment mechanics can also explain the difficulties to detect alterations in starch fine structure in the transgenic lines
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additional information
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construction of deletion GtfB-DELTANDELTAV mutant D1015N
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additional information
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construction of a GtfB enzyme 4,6-alpha-glucanotransferase lacking 761 N-terminal amino acids
additional information
Streptococcus thermophilus NCC2408
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construction of a GtfB enzyme 4,6-alpha-glucanotransferase lacking 761 N-terminal amino acids
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