• Bulletin of the Korean Chemical Society
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• v.26 no.4
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• pp.679-681
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• 2005

• Applied Biological Chemistry
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• v.6
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• pp.107-117
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• 1965

(1) In order to study the specificity of Aspergillus soya protease to soybean protein, as well as the types of peptides formed during soybean-koji prerapation the amino acid sequence for the di & tripeptide and N-terminal amino acid residue and C-terminal amino acid residue were identified. As the results of the study, the following were obtained. Gly, Glu. Ala. Ser. Glu. Ser. Ala. Val (Cys, Glu, Ser, Ala, Arg, Try, Leu or Ileu) Asp. Phe (His, Arg, Cys, Asp, Ser, Ala, Leu or Ileu) Glu. Ala (Cys, Gly, Met) Glu. Ala (Asp, Glu,) Gly. Met (Asp, Glu, Ala, Tyr, Leu or Ileu, Lys,) Gly. Leu or Ileu (His, Asp, Glu, Gly, Ser, Lys, Thr, Phe,) Cys. Gly (Asp, Tyr,) Glu. Pro (Asp, Glu, Ser, Gly, Thr, Ala, Val, Leu or Ileu) Try. Ser (Gly, Glu, Arg, Ala, Met, Leu or Ileu,) Asp. Met (Asp, Glu, Ala, Try, Pro, Leu or Ileu,) His Thr (Ser, Gly, Tyr, Pro, Leu or Ileu,) Glu. Gly (Asp, Ala, Ser, Glu,) Leu or Ileu (2) It has revealed that Aspergillus soya protease has considerably wider range of specificity than that of chymotrypsin, pepsin and trypsin but not mold protease and Aspergillus saitoi protease. It can be said that Asp. soya protease split the bond adjacent to glutamic acid, aspartic acid, glycine, serine, alanine, cystine, tryptophan, histidine preferably acidic amino acid as C-terminal amino acid residue.

• Bulletin of the Korean Chemical Society
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• v.28 no.5
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• pp.840-842
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• 2007

• Journal of Life Science
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• v.22 no.3
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• pp.306-311
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• 2012

A gene encoding a lipase, lipT, was cloned from the psychrotrophic bacterium Pseudomonas mandelii and sequenced. An open reading frame of 1,686 bp was found that encodes a polypeptide consisting of 562 amino acid residues. Sequence analysis revealed a Gly-His-Ser-Leu-Gly sequence, which matches the consensus Gly-X-Ser-X-Gly motif conserved among lipolytic enzymes. The recombinant LipT protein was predominantly expressed as inclusion bodies in Escherichia coli and subsequently purified by nickel-chelate affinity chromatography. A small fraction of LipT was refolded, and the subsequent LipT exhibited substrate preferences for p-nitrophenyl butyrate (C4) and p-nitrophenyl octanoate (C8).

• Journal of the Korean Chemical Society
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• v.46 no.1
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• pp.46-51
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• 2002

The recognition and cleavage of 5S rRNA from P. alcaligenes by metallopeptides to the form $Ni(II){\cdot}Gly$-Gly-His(Arg)COOH and $Cu(II){\cdot}Gly$-Gly-His(Arg)COOH were investigated. The results of RNA cleavage analyses suggest that metallopeptides selectively target the unpaired or unstably paired bases of stem-loop structure of 5S rRNA. The selectivity of metallopeptides was little affected by the species of metal ion, Ni(II) or Cu(II). When the result of cleavage by metallopeptides was compared with that of by metal complexes M(II)CR, the recognition by metallopeptides was more selective and structure specific. The cleavage data by metallopeptides and other metal complexes were used to probe the secondary structure of 5S rRNA from P. alcaligenes.

• Journal of Microbiology and Biotechnology
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• v.26 no.6
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• pp.1077-1086
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• 2016

Glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone (DHA). The gldA gene encoding a putative GlyDH was cloned from Thermoanaerobacterium thermosaccharolyticum DSM 571 (TtGlyDH) and expressed in Escherichia coli. The presence of Mn²⁺ enhanced its enzymatic activity by 79.5%. Three highly conserved residues (Asp¹⁷¹, His²⁵⁴, and His²⁷¹) in TtGlyDH were associated with metal ion binding. Based on an investigation of glycerol oxidation and DHA reduction, TtGlyDH showed maximum activity towards glycerol at 60℃ and pH 8.0 and towards DHA at 60℃ and pH 6.0. DHA reduction was the dominant reaction, with a lower K_m(DHA) of 1.08 ± 0.13 mM and V_max of 0.0053 ± 0.0001 mM/s, compared with glycerol oxidation, with a K_m(glycerol) of 30.29 ± 3.42 mM and V_max of 0.042 ± 0.002 mM/s. TtGlyDH had an apparent activation energy of 312.94 kJ/mol. The recombinant TtGlyDH was thermostable, maintaining 65% of its activity after a 2-h incubation at 60℃. Molecular modeling and site-directed mutagenesis analyses demonstrated that TtGlyDH had an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg⁴³, both related to dinucleotide binding.

• Journal of Aquaculture
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• v.15 no.3
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• pp.157-163
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• 2002

Thirteen groups, each consisting of 25 juveniles (0.64 g) of the Korean rockfish, Sebastes schlegeli were reared in aquaria after period of one week conditioning. Each group was fed with one of the 13 diets at the rate of 7~10% body weight (on a dry-matter basis) 2 times a day for 6 weeks. Each diet was supplemented with one of the following amino acids at 3g/kg diet: Alanine (Ala), Arginine (Arg), Glycine(Gly), Glutamate (Glu), Histidine (His), Isoleusine(Ile), Lysine (Lys), Methionine (Met), Phenylalanine (Phe), Proline (Pro), Threonine (Thr), Tryptophan (Trp) or Valine (Val). Groups fed with Pro, Thr, Met or Gly-supplemented diet showed significantly (p<0.05) higher weight gain and faster specific growth rate than the groups fed on other diets, while those fed Pro, Thr, Met or Gly were not significantly different each other(P>0.05). Feed efficiency (FE) of fish fed Pro was significantly higher than those fed the other diets except that fed Thr (P<0.05). However, there was no significant difference between FE of fish fed Pro and Thr, and among FE of fish fed Thr, Met and Gly (P>0.05). The requirement of rockfish is higher for Met and Thr. Extra Pro and/or Gly may also stimulate biosynthesis of the nucleic acids (IMP, GMP) which are known as the feed stimulant in fish.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.30 no.3 s.47
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• pp.399-404
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• 2004

Novel GHK-conjugated chitosan was prepared by the solid-phase method using $N^{\alpha}-Fmoc$ amino acids/BOP coupling reagent. For this purpose, the chitosan microbeads which had a mean diameter of 70 um were prepared by the W/O emulsion-phase separation method. The GHK was successfully coupled to the chitosan microbeads by stepwise solid-phase method. The result of amino aid analysis was in good agreement with the theoretical values; $Gly_{1.02}\;of\;His_{1.13}\;Lys_{0.96).$. The cell proliferation effect of the GHK-bound chitosan microbeads was measured by MTT assay. We concluded that GHK-bound chitosan microbeads gave higher cell Proliferation effect than chitosan microbeads.

• Bulletin of the Korean Chemical Society
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• v.30 no.2
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• pp.409-414
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• 2009

Novel binol aldehydes derivatized at 2' hydroxy position with both uryl and acetamide groups (2), and diuryl groups (3) have been synthesized. Both were designed for streospecific binding and chirality conversion of general dipeptides with support of multiple hydrogen bonding donor sites in the receptors. The receptors, 2 and 3, converted the chirality of N-terminal amino acids of peptides such as Ala-Gly, Met-Gly, Leu-Gly and His-Gly with stereoselectivity on D-form over L-form. The stereoselectivity ratios were in the range of 5-11, somewhat higher than those of the binol receptor with mono uryl group (1). The DFT calculation at the B3LYP/6-31G$^*$//MPWB1K/6-31G$^*$ level revealed that 3-D-Ala-Gly was 2.2 kcal/mol more stable than 3-L-Ala-Gly. The considerable steric hindrance between the methyl group of the alanine and the imine CH moiety of the receptor seems to be the main contributing factor for the thermodynamic preference.

• Applied Biological Chemistry
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• v.15 no.2
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• pp.111-142
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• 1972

An experimental Chung-Kook-Jang was prepared using the strain Bacillus subtilis sp. isolated by the author Samples were taken in 12 hrs interval during the fermentation and the oligopeptides were separated by the method of molecular sieving using the ion exchange resin column of Dowex-50. Only the X-16 fraction of oligopeptides was taken and the components of oligopeptides were developed in two dimensional thin layer chromatograms. The each peptide spot was eluted and each peptide was isolated. The pattern and kinds of amino acids, and N and C-terminal amino acids were studied. Fourteen different oligopeptides could be detected by the two dimensional thin layer chromatography, all of which were consisted of $4{\sim}9$ kinds of amino acids. No dipeptides and no tripeptides could be found. The N and C-terminal amino acids and the residual component amino acids of all these 14 peptides could be summarized as the follows. [P]-I. Pro (Cys Ala Asp Trp Ile Val) Glu [P]-II. Val (His Arg Glu Thr Ala Met) Asp [P]-III. Glu (Cys Lys Asp Thr Met) Ala [P]-IV. Glu(His Ser Ala) Met) [P]-V. Ile (Cys Asp Arg Gly Pro T.p Phe) His [P]-VI. Gly(Asp ser) Lys [P]-VII. Thr(Pro Tyr Phe) Asp [P]-VIII. Phe(Tyr Leu Ile) Val [P]-IX. Trp (Phelle) Thr [P]-X. Ile (Arg Leu) Phe [P]-XI. Asp (Lys His Ser Gly Glu Pro) Ala [P]-XII. Glu (Cys Asp Gly) Ser [P]-XIII. Ala (Arg Tyr) Glu [P]-XIV. Met (Glu Ala) His It appears that the protease of the Bacillus subtilis K-27 syrain has rather wider range of specificity than proteases of Aspergoillus soya, pepsin, chymotrypsin, and trypsin.