Sequence conservation of the catalytic regions of anylolytic enzymes in maize branching enzyme-I

Baba, Tadashi; Kimura, Koji; Mizuno, Kouichi; Etoh, Hirotoshi; Ishida, Yoshiki; Sato, Osamu

doi:10.1016/s0006-291x(05)81385-3

Cited by 109 publications

(62 citation statements)

References 24 publications

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“…Peptide 9 differed from the deduced amino acid sequences of the BE 7 as well as of the BE 71 clone by having a Phe residue instead of a Cys residue in the first position. Our sequence data show that the 97 kDa and 103 kDa forms of potato branching enzyme are highly similar to isoform I of the enzyme from maize endosperm [9] (Table II). Three out of four of the internal peptides (Pl, P2 and P6) from the middle third of the enzyme are identical to corresponding sequences in the maize enzyme.…”

Section: N-terminal Sequencing Of Sbementioning

confidence: 69%

“…These discrepancies might be due to misincorporation by the Taq polymerase but they could also reflect polymorphism (see section 4). The deduced amino acid sequence of the PCR fragment was 82% and 80% iden- Table II Comparison of peptides Pl-P9 of potato tuber SBE I with the corresponding amino acid sequences deduced from the BE 7 and BE 7i potato cDNA clones [23] and a maize SEE I cDNA clone (Ml) [9] Peptide Sequence R..N.................Y.v..~-ass 3a&...R..N.................Y Nucleotide sequence the deduced acid sequence of a PCR-fragment encoding part of SBE I with the amino acid of maize [9] and (R) [S] I. The peptides (PI PS) from the PCR primers were are underlined The additional and sequenced (P2, P6 P7), included the PCR-fragment, underlined twice, differences between PCR-fragment nucleotide and the 7 and 71 cDNA [23] are (*).…”

Section: Isolation Of An Internal Cdna Fragment Coding For Potato Sbementioning

confidence: 99%

“…The peptides (PI PS) from the PCR primers were are underlined The additional and sequenced (P2, P6 P7), included the PCR-fragment, underlined twice, differences between PCR-fragment nucleotide and the 7 and 71 cDNA [23] are (*). Of differences three in amino substitutions: Ser 38) for in BE Ser (nt for Gly BE 7 Lys (nt for Arg both BE and BE tical to the primary sequence of SBE I from maize [9] and rice [8], respectively (Fig. 3). …”

Section: Isolation Of An Internal Cdna Fragment Coding For Potato Sbementioning

confidence: 99%

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Characterization of the 97 and 103 kDa forms of starch branching enzyme from potato tubers

Khoshnoodi

Rask

et al. 1993

FEBS Letters

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Terminal analysis, peptide mapping and partial peptide sequencing of the 97 and 103 kDa forms of starch branching enzyme from potato tubers showed that the two forms are highly related. A comparison with sequence data in the literature showed that these forms belong to the starch branching enzyme isofonn I family. An internal cDNA fragment was obtained using PCR technology on potato tuber RNA with two oligonucleotide primers constructed from the peptide sequence data. Southern blot analysis using the PCR fragment as probe showed that there is only one gene locus encoding this isofonn of the enzyme in Solarturn tuberosum as well as in Solanum commersonii.

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Section: N-terminal Sequencing Of Sbementioning

confidence: 69%

Section: Isolation Of An Internal Cdna Fragment Coding For Potato Sbementioning

confidence: 99%

Section: Isolation Of An Internal Cdna Fragment Coding For Potato Sbementioning

confidence: 99%

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Characterization of the 97 and 103 kDa forms of starch branching enzyme from potato tubers

Khoshnoodi

Rask

et al. 1993

FEBS Letters

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“…However, the overall identities are still low (29 and 37% identities for GBSSI and GBSSII, respectively). It has been shown that branching enzyme, which is able to catalyze the formation of branches with a-l,6-glucosidic linkages, conserves four consensus sequences of the catalytic sites of amylolytic hydrolases, in spite of the fact that branching enzyme belongs to a family of transferases (Baba et al, 1991;Mizuno et al, 1992Mizuno et al, , 1993. Soluble starch synthase, as well as glycogen synthase, however, possesses no conserved sequence of the four catalytic sites in the amylolytic enzymes (Figs.…”

Section: Discussionmentioning

confidence: 99%

Identification, cDNA Cloning, and Gene Expression of Soluble Starch Synthase in Rice (Oryza sativa L.) Immature Seeds

et al. 1993

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Three forms of soluble starch synthase were resolved by anionexchange chromatography of soluble extracts from immature rice (Oryza safiva 1.) seeds, and each of these forms was further purified by affinity chromatography. The 55-, 57-, and 57-kD proteins in the three preparations were identified as candidates for soluble starch synthase by western blot analysis using an antiserum against rice granule-bound starch synthase. It is interesting that the aminoterminal amino acid sequence was identical among the three proteins, except that the 55-kD protein lacked eight amino acids at the amino terminus. Thus, these three proteins are products of the same gene. lhe cDNA clones coding for this protein have been isolated from an immature rice seed library in Agtll using synthetic oligonucleotides as probes. The deduced amino acid sequence of this protein contains a lysine-X-glycine-glycine consensus sequence for the ADP-glucose-binding site of starch and glycogen synthases. Therefore, we conclude that this protein corresponds to a form of soluble starch synthase in immature rice seeds. The precursor of the enzyme contains 626 amino acids, including a 113-residue transit peptide at the amino terminus. lhe mature form of soluble starch synthase shares a significant but low sequence identity with rice granule-bound starch synthase and Escherichia coli glycogen synthase. However, several regions, including the substrate-binding site, are highly conserved among these three enzymes. Blot hybridization analysis demonstrates that the gene encoding soluble starch synthase is a single-copy gene in the rice genome and is expressed in both leaves and immature seeds. These results suggest that soluble and granule-bound starch synthases play distinct roles in starch biosynthesis of plant.

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“…The structures of both enzymes are based on a similar (␣/␤) 8 barrel as their main domain, and they have common amino acid residues which may act as catalytic sites (6,7,10). The primary structural analyses (1,(11)(12)(13)(14) and the secondary structural predictions (15,16) suggest a close relationship of the threedimensional structures for the enzymes which catalyze all of the above mentioned reactions.…”

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confidence: 99%

Controlling Substrate Preference and Transglycosylation Activity of Neopullulanase by Manipulating Steric Constraint and Hydrophobicity in Active Center

Kuriki

Kaneko

Yanase

et al. 1996

Journal of Biological Chemistry

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The substrate specificity and the transglycosylation activity of neopullulanase was altered by site-directed mutagenesis on the basis of information from a threedimensional structure predicted by computer-aided molecular modeling. According to the predicted three-dimensional structure of the enzyme-substrate complex, it was most likely that Ile-358 affected the substrate preference of the enzyme. Replacing Ile-358 with Trp, which has a bulky side chain, reduced the acceptability of ␣-(136)-branched oligo-and polysaccharides as substrates. The characteristics of the I358W-mutated enzyme were quite different from those of wild-type neopullulanase and rather similar to those of typical starch-saccharifying ␣-amylase. In contrast, replacing Ile-358 with Val, which has a smaller side chain, increased the preference for ␣-(136)-branched oligosaccharides and pullulan as substrates. The transglycosylation activity of neopullulanase appeared to be controlled by manipulating the hydrophobicity around the attacking water molecule, which is most likely used to cleave the glucosidic linkage in the hydrolysis reaction. We predicted three residues, Tyr-377, Met-375, and Ser-422, which were located on the entrance path of the water molecule might be involved. The transglycosylation activity of neopullulanase was increased by replacing one of the three residues with more hydrophobic amino acid residues; Y377F, M375L, and S422V. In contrast, the transglycosylation activity of the enzyme was decreased by replacing Tyr-377 with hydrophilic amino acid residues, Asp or Ser.

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Sequence conservation of the catalytic regions of anylolytic enzymes in maize branching enzyme-I

Cited by 109 publications

References 24 publications

Characterization of the 97 and 103 kDa forms of starch branching enzyme from potato tubers

Characterization of the 97 and 103 kDa forms of starch branching enzyme from potato tubers

Identification, cDNA Cloning, and Gene Expression of Soluble Starch Synthase in Rice (Oryza sativa L.) Immature Seeds

Controlling Substrate Preference and Transglycosylation Activity of Neopullulanase by Manipulating Steric Constraint and Hydrophobicity in Active Center

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