On the Mechanism and Stereochemistry of the Malate-Lactate Fermentation of Leuconostoc mesenteroides (1)

On the Mechanism and Stereochemistry of the Malate-Lactate Fermentation of Leuconostoc... Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1209 - 1214, September 1976 On the Mechanism and Stereochemistry of the Malate-Lactate Fermentation of Leuconostoc mesenteroidesM Adolf KRAUS, Waltraud DESSAU and Helmut SIMON Organisch-Chemisches Institut der Technischen Universität München (Received 8 June 1976) Summary: During the transformation of (25, 3R) [3-3H]malate to (5) lactate no tritium exchange takes place. The stereochemical course of the decarboxylation studied with (25,3 R) [3-2H]malate in 3HOH/H20 and (2 S, 3 R) [3-3H]malate in 2H20 occurs with retention and is therefore the same as that determined by other authors for malic enzyme from vertebrates and ftomEscherichia coll The malate-lactate fermentation is a useful procedure to prepare chiral methyl groups on a preparative scale starting from (2S, 3 R] [3-H]malate. Über den Mechanismus und die Stereochemie der Malat-Lactat-Fermentation von Leuconostoc mesenteroides Zusammenfassung: Die Umwandlung von (25, 3 R) [2-3H]Malat in (S)Lactat erfolgt ohne Tritiumaustausch. Die Decarboxylierung von Malat wurde mit (25, 3R) [3-2H]Malat in 3 HOH/H20 und mit (2S, 3 /?) [3-3H]Malat in 2 H20 untersucht. Sie verläuft unter Retention und ist damit identisch mit der, die von anderen Autoren für das Malatenzym aus Vertebraten bzw. aus Escherichia coli gefunden wurde. Die Malat-Lactat-Fermentation ist ein brauchbares http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

On the Mechanism and Stereochemistry of the Malate-Lactate Fermentation of Leuconostoc mesenteroides (1)

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.2.1209
Publisher site
See Article on Publisher Site

Abstract

Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1209 - 1214, September 1976 On the Mechanism and Stereochemistry of the Malate-Lactate Fermentation of Leuconostoc mesenteroidesM Adolf KRAUS, Waltraud DESSAU and Helmut SIMON Organisch-Chemisches Institut der Technischen Universität München (Received 8 June 1976) Summary: During the transformation of (25, 3R) [3-3H]malate to (5) lactate no tritium exchange takes place. The stereochemical course of the decarboxylation studied with (25,3 R) [3-2H]malate in 3HOH/H20 and (2 S, 3 R) [3-3H]malate in 2H20 occurs with retention and is therefore the same as that determined by other authors for malic enzyme from vertebrates and ftomEscherichia coll The malate-lactate fermentation is a useful procedure to prepare chiral methyl groups on a preparative scale starting from (2S, 3 R] [3-H]malate. Über den Mechanismus und die Stereochemie der Malat-Lactat-Fermentation von Leuconostoc mesenteroides Zusammenfassung: Die Umwandlung von (25, 3 R) [2-3H]Malat in (S)Lactat erfolgt ohne Tritiumaustausch. Die Decarboxylierung von Malat wurde mit (25, 3R) [3-2H]Malat in 3 HOH/H20 und mit (2S, 3 /?) [3-3H]Malat in 2 H20 untersucht. Sie verläuft unter Retention und ist damit identisch mit der, die von anderen Autoren für das Malatenzym aus Vertebraten bzw. aus Escherichia coli gefunden wurde. Die Malat-Lactat-Fermentation ist ein brauchbares

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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