| | 1 | Author
| Siegrid Schoch3, M. Onica Ihl | Requires cookie* | | | Title
| Substrate Specificity of Chlorophyllase from Different Plants  | | | | Abstract
| The activity of chlorophyllase (chlorophyll-chlorophyllido-hydrolase, EC 3.1.1.14) ex tracted from six different species was com pared with enzyme extracted from leaves of Tree of Heaven. The chlorophyllase activity from Swiss chard was similar to the Tree of Heaven enzyme, all the others were less active or inactive. We tested the substrate specificity with bacteriochlorophyll a, chlorophylls a and b. pheophytins a and b and also the synthetic pig ments Zn pheophytins a and b and Zn pyropheophytin a. The natural pigments were the best substrates, but the Zn derivatives were also hydrolysed, except Zn pyropheophytin a which was accepted only by the enzyme extracted from the leaves of Tree of Heaven. | | | |
Reference
| Z. Naturforsch. 53c, 21 (1998); received Septem ber 19/October 11 1997 | | | |
Published
| 1998 | | | |
Keywords
| Chlorophyll, Chlorophyllase, Substrates Specificity, Vegetables, Zn pheophytin | | | |
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| default:Reihe_C/53/ZNC-1998-53c-0021.pdf | | | | Identifier
| ZNC-1998-53c-0021 | | | | Volume
| 53 | |
| 2 | Author
| KenjiM. Atsui, Hiroyuki Shinta, H. Irom, Itsu Toyota, Tadahiko Kajiwara, AkikazuH. Atanaka | Requires cookie* | | | Title
| Comparison of the Substrate Specificities of Lipoxygenases Purified from Soybean Seed, Wheat Seed, and Cucumber Cotyledons | | | | Abstract
| Lipoxygenases were highly purified from soybean seed, wheat seed and cucumber cotyle dons. Substrate specificities o f these lipoxygenases were studied by using an entire series o f (co6Z ,co9Z)-C 13~C24-dienoic acids as synthetic substrate analogues. Soybean lipoxygenase-1 and cucumber lipoxygenase showed broad specificities for these substrates while wheat lipoxygenase showed narrow specificities. Position o f dioxygenation to each substrate was an alyzed by high performance liquid chromatography. W ith soybean lipoxygenase-1 elongation o f the distance between the terminal carboxyl group and the site o f hydrogen removal in a substrate decreased the positional specificity o f dioxygenation, while, with cucumber lipoxy genase, shortening the distance decreased the specificity. It was suggested that cucumber lipoxygenase and soybean lipoxygenase-1 recognized the terminal carboxyl group o f a sub strate to arrange it only in one orientation at the reaction center. In case o f wheat lipoxygen ase, recognition o f the carboxyl group was thought to have crucial and essential role to secure the activity. | | | |
Reference
| Z. Naturforsch. 47c, 85—8 (1992); received M ay 8/A ugust 27 1991 | | | |
Published
| 1992 | | | |
Keywords
| Lipoxygenase, Cucumber Cotyledons, Soybean Seed, W heat Seed, Substrate Specificity | | | |
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| default:Reihe_C/47/ZNC-1992-47c-0085.pdf | | | | Identifier
| ZNC-1992-47c-0085 | | | | Volume
| 47 | |
| 3 | Author
| AkikazuH. Atanaka, T. Adahiko Kajiwara, Kenji Matsui, Hiromitsu Toyota | Requires cookie* | | | Title
| Substrate Specificity of Tea Leaf Hydroperoxide Lyase | | | | Abstract
| Substrate specificity o f tea leaf fatty acid hydroperoxide lyase was systematically investigat ed using an entire series o f co6-(5)-hydroperoxy-C14-C24 dienoic and trienoic acids as sub strates. Unexpectedly, the hydroperoxides o f C22 but not natural substrates, i.e., those o f C 18, showed the highest reactivities for the lyase. The reactivities o f the hydroperoxides o f trienoic acids were always four to ten times higher than those o f the dienoic acids. | | | |
Reference
| Z. Naturforsch. 47c, 677—6 (1992); received June 24/July 24 1992 | | | |
Published
| 1992 | | | |
Keywords
| Aldehyde, Fatty Acid Hydroperoxide, Hydroperoxide Lyase, Substrate Specificity, Tea Leaf | | | |
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| default:Reihe_C/47/ZNC-1992-47c-0677.pdf | | | | Identifier
| ZNC-1992-47c-0677 | | | | Volume
| 47 | |
| 4 | Author
| PaulL D Urham, JonathanE. Poulton | Requires cookie* | | | Title
| Enzymic Properties of Purified Myrosinase from Lepidium sativum Seedlings | | | | Abstract
| To establish the substrate specificity o f the thioglucoside glucohydrolase myrosinase (EC 3.2.3.1), this enzyme was purified to homogeneity from light-grown cress (Lepidium sativum L.) seedlings by Sephadex gel filtration. Red Dye and anion exchange (FPLC M ono Q) chro matography, and preparative isoelectric focusing. Hydrolytic activity was shown toward only 4 o f the 29 synthetic and natural O-and S-glycosides tested. Highest activity was displayed with the endogenous glucosinolates benzylglucosinolate (ATm, 295 |iM) and sinigrin (K ml 300 |iM) at an optimum pH o f 5.5 in sodium citrate buffer. The synthetic glycosides PNPG (K m, 2.0 m M) and ONPG were poorer substrates at an optimum pH o f 6.5 in potassium phos phate buffer. The enzyme was inactive with all other nitrophenyl glycosides tested including PNP-a-D-glucoside and PNP-thio-ß-D-glucoside, suggesting a requirement for O-ß-D-glucose as the glycone moiety within these substrates. PNPG hydrolysis was stimulated 2.6-fold by ascorbate (1 m M). The enzyme exhibited no metal ion requirement and was strongly inhibited by lead nitrate, mercury chloride, and ferric chloride at 1 m M concentration. The metal chela tors D IE C A , ED TA , o-phenanthroline, and 2,2'-dipyridyl were not inhibitory, but the thiol reagents PCM S, PCMB, and N-ethylmaleimide (at 1 m M) caused 5 0 -8 0 % inhibition o f enzyme activity. | | | |
Reference
| Z. Naturforsch. 45c, 173—178 (1990); received September 9 1989 | | | |
Published
| 1990 | | | |
Keywords
| Lepidium sativum, Thioglucoside Glucohydrolase, M yrosinase, Substrate Specificity, Gluco-sinolate Degradation | | | |
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| default:Reihe_C/45/ZNC-1990-45c-0173.pdf | | | | Identifier
| ZNC-1990-45c-0173 | | | | Volume
| 45 | |
| 5 | Author
| Abteilung Biochemie, C.H Boehringer Sohn | Requires cookie* | | | Title
| B. Schöbel und W. Pollmann | | | | Abstract
| In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamid gelelectrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamid gelelectrophoresis showed a molecular weight of 60000, demonstrating four subunits o f the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature o f 55 °C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms. Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger | | | |
Reference
| Z. Naturforsch. 35c, 699—701 (1980); eingegangen am 12. Mai/20. Juni 1980 | | | |
Published
| 1980 | | | |
Keywords
| Chlorogenic Acid Hydrolase, Aspergillus niger, Polyacrylamid Gelelectrophoresis, Amino Acid Analysis, Substrate Specificity | | | |
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| default:Reihe_C/35/ZNC-1980-35c-0699.pdf | | | | Identifier
| ZNC-1980-35c-0699 | | | | Volume
| 35 | |
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