Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.4.1.18 (branching enzyme)
 628 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

High glycogen content and abnormal mitochondria have been seen in muscles from RN- carrier pigs in a previous work. Glycogen synthase, branching enzyme, phosphorylase and debranching enzyme activities, and mitochondrial characteristics were studied in normal and RN- carrier pigs. Branching enzyme activity was higher (P < 0.01) and glycogen synthase activity tended to be higher in longissimus dorsi muscle from RN- carrier pigs compared to normal pigs. There were no differences in the activities of either phosphorylase and debranching enzyme between both types of pigs. Citrate synthase activity and mitochondrial respiration were slightly higher in muscle from RN- pigs compared to normal pigs. Glycogen content in muscle from RN- pigs could result from the imbalance between anabolic and catabolic enzyme activities of glycogen metabolism. The higher specific activity in mitochondria of RN- pigs muscle might be the compensatory effect of an abnormal glycolytic metabolism.
Comp Biochem Physiol Biochem Mol Biol 1994 Jul
PMID:Enzyme activities of glycogen metabolism and mitochondrial characteristics in muscles of RN- carrier pigs (Sus scrofa domesticus). 808 56

The wrinkled-seed mutant (rr) of pea (Pisum sativum L.) arose through mutation of the gene encoding starch-branching enzyme isoform I (SBE1) by insertion of a transposon-like element into the coding sequence. Two isoforms of starch-branching enzyme have been documented in the developing pea embryo. The second isoform, SBEII, is expressed towards the later stages of embryo development while SBEI is expressed highly in the early stages. Due to mutation of SBEI the total amount of starch and the proportion of amylopectin, a branched starch polymer, are greatly reduced in the wrinkled (rr) line as compared to that in the wild-type, round (RR) line. Consequently, the level of sucrose in the rr line is nearly two fold that of the RR line. Increased sucrose concentration in the developing embryos of this mutant line causes increased uptake of water and thereby increases the cell size and fresh weight. During seed maturation in these mutant seeds a greater loss of water occurs. As a result, the wrinkled seed phenotype develops. Besides this morphological variation, the mutation also causes changes in the amount of lipid and of one storage protein, legumin. This review article discusses the role of the SBEI enzyme in causing such metabolic changes in the developing embryos with the implication that metabolism can play a central role in plant development.
Plant Mol Biol 1993 Jun
PMID:The importance of starch biosynthesis in the wrinkled seed shape character of peas studied by Mendel. 832 88

The sequence of a rice gene encoding a starch branching enzyme (sbe1) shows extreme divergence from that of the rice gene, that is homologous to bacterial glycogen branching enzyme (sbe2). sbe1 is expressed abundantly and specifically in developing seeds and maximally in the middle stages of seed development. This expression pattern completely coincides with that of the waxy gene, which encodes a granule-bound starch synthase. Three G-box motifs and consensus promoter sequences are present in the 5' flanking region of sbe1. It encodes a putative transit peptide, which is required for transport into the amyloplast. A 2.2 kb intron (intron 2) precedes the border between the regions encoding the transit peptide and the mature protein, and contains a high G/C content with several repeated sequences in its 5' half. Although only a single copy of sbe1 is present in the rice genome, Southern analysis using intron 2 as a probe indicates the presence of several homologous sequences in the rice genome, suggesting that this large intron and also the transit peptide coding region may be acquired from another portion of the genome by duplication and insertion of the sequence into the gene.
Mol Gen Genet 1993 Feb
PMID:Molecular analysis of the gene encoding a rice starch branching enzyme. 845 48

Using a cDNA library prepared from poly(A)+ RNA from 10-day-old rice endosperm, partial nucleotide sequences of randomly isolated clones were analyzed. A total of 153 (30.6%) out of 500 cDNA clones showed high amino acid identity to previously identified genes. There was significant redundancy in cDNAs encoding prolamine and glutelin. About 21.0% of the cDNA clones were found to code for seed storage protein genes. Consequently, 37 independent genes were identified. Using cDNA clones encoding glutelin, prolamine, seed allergen, alpha-1,4-glucan branching enzyme, glycine-rich RNA binding protein, metallothionein, non-specific lipid-transfer protein and ubiquitin conjugating enzyme the accumulation of mRNA during rice seed development was compared. Genes associated with seed storage protein and starch biosynthesis were expressed according to expected developmental stages. Glycine-rich RNA binding protein genes as well as metallothionein-like protein genes were highly expressed in developing seeds, but low in leaves of whole plants.
Plant Mol Biol 1995 Nov
PMID:Analysis of randomly isolated cDNAs from developing endosperm of rice (Oryza sativa L.): evaluation of expressed sequence tags, and expression levels of mRNAs. 854 95

In the overtly differentiated colonies of Streptomyces coelicolor A3(2), discrete phases of glycogen synthesis are found at the vegetative/aerial mycelium boundary (phase I) and in the immature spore chains at aerial hyphal tips (phase II). We have characterized two S. coelicolor glgB genes encoding glycogen branching enzyme, which are well separated in the genome. Disruption of glgBl led to the formation of abnormal polyglucan deposits at phase I, with phase II remaining normal, whereas disruption of glgBII interfered specifically with phase II deposits, and not with those of phase I. Thus, each branching enzyme isoform is involved in a different phase of glycogen synthesis. This situation contrasts with that in simple bacteria, which typically have a single set of enzymes for glycogen metabolism, and more closely resembles that in plants.
Mol Microbiol 1995 Oct
PMID:Tissue-specific glycogen branching isoenzymes in a multicellular prokaryote, Streptomyces coelicolor A3(2). 859 63

Two starch branching enzyme (SBE) cDNAs were identified in an Arabidopsis seedling hypocotyl library using maize Sbe1 and Sbe2 cDNAs as probes. The two cDNAs have diverged 5' and 3' ends, but encode proteins which share 90% identity over an extensive region with 70% identity to maize SBE IIb [12]. Genomic Southern blots suggest that the two cDNAs are the products of single, independent genes, and that additional, more distantly related SBE genes may exist in the Arabidopsis genome. The two cDNAs hybridize to transcripts which show similar expression patterns in Arabidopsis vegetative and reproductive tissues, including seedlings, inflorescence rachis, mature leaves, and flowers. This is the first report of the identification of cDNAs encoding two closely related starch branching enzymes from the same species.
Plant Mol Biol 1996 Jan
PMID:Two closely related cDNAs encoding starch branching enzyme from Arabidopsis thaliana. 861 46

Expression of the maize (Zea mays L.) starch branching enzyme (SBE) genes Sbe1 and Sbe2 were characterized during kernel development and in vegetative tissues. The onset of Sbe1 and Sbe2 expression during endosperm development was similar to that of other genes involved in starch biosynthesis (Wx, Sh2 and Bt2). However, the expression of Sbe2 peaked earlier than that of Sbe1 in developing endosperm and embryos resulting in a shift in the ratio of Sbe1 to Sbe2 relative message levels during kernel and embryo development. Transcripts hybridizing to the Sbe2 probe were not detectable in leaves or roots which nonetheless have SBEII enzymatic activity, suggesting that there may be another divergent SBEII-like gene(s) in maize. A similar expression pattern is shared between the maize genes and related genes in pea, which together with their evolutionary conservation, suggests that the SBE isoforms may play unique roles in starch biosynthesis during plant development.
Plant Mol Biol 1996 Mar
PMID:Evolutionary conservation and expression patterns of maize starch branching enzyme I and IIb genes suggests isoform specialization. 870 31

Different branching enzymes were partially purified in order to get some insight into their mechanism of action. Each branching enzyme is able to synthesize in vitro at any moment, even during very short incubation times, only one type of alpha 1,4-alpha 1,6 glucopolysaccharide, which possesses unique and specific properties (lambda max; A; R;% of beta-amylolysis;% alpha 1,6). Between two branching points, each branching enzyme will leave, in average, a constant and specific number of glucoses alpha 1,4-linked, which is characteristic of that particular enzyme. Consequently the structure of the polysaccharide will keep the same independently from the moment of synthesis.
Cell Mol Biol (Noisy-le-grand) 1996 Jul
PMID:Differential action of branching enzymes according to its source. 883 89

Full-length cDNA for starch branching enzyme (SBE) II of potato was isolated and sequenced. In potato, similarly to most other investigated plants, the SBE-II isoform differs from SBE-I by having an acidic amino-terminal extension and a shorter carboxyterminus. Two forms of SBE-II, migrating as 98 and 95 kDa proteins in 6% SDS-polyacrylamide gels, were associated to tuber starch. The latter form was 16 amino acids shorter in the amino terminus. Transcript of SBE-II was present in leaf tissue, whereas significant expression was not seen in tubers. On the other hand, a significant amount of SBE-I transcript was detected in tuber tissue but not in leaves.
Plant Mol Biol 1998 Jun
PMID:Molecular cloning and characterization of starch-branching enzyme II from potato. 961 17

Rat brain glycogen branching enzyme was partially purified in order to elucidate its mechanism of action. The alpha1,4-alpha1,6-glucan polysaccharide was synthesized using rat brain branching enzyme under two different elongation conditions: Glc-1-P and phosphorylase or UDP-Glc and glycogen synthase. The products obtained demonstrated that the cpolysaccharides synthesized (pattern of the spectra obtained in the presence of Krisman's reagent, lambda max, parameter A and R, % beta-amylolysis and degree of branching) under different incubation times are nearly constant. These results imply that the degree of branching of a polysaccharide depends only on the enzyme specificity.
Cell Mol Biol (Noisy-le-grand) 1998 May
PMID:Glycogen brain branching enzyme. 962 Apr 41


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