論文

査読有り 筆頭著者 責任著者
2015年6月

Aldolase as a Chirality Intersection of L-Amino Acids and D-Sugars

ORIGINS OF LIFE AND EVOLUTION OF BIOSPHERES
  • Toratane Munegumi

45
1-2
開始ページ
173
終了ページ
182
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1007/s11084-015-9415-8
出版者・発行元
SPRINGER

Aldolase plays an important role in glycolysis and gluconeogenesis to produce D-fructose-1,6-bisphosphate (D-FBP) from dihydroxyacetone phosphate (DHP) and D-glyceraldehyde-3-phosphate (D-GAP). This reaction is stereoselective and retains the D-GAP 2R configuration and yields D-FBP (with the configuration: 3S, 4S, 5R). The 3- and 4-position carbons are the newly formed chiral carbons because the 5-position carbon of D-FBP comes from the 2-position of D-GAP. Although four diastereomeric products, (3S, 4R, 5R), (3R, 4R, 5R), (3R, 4S, 5R), (3S, 4S, 5R), are expected in the nonenzymatic reaction, only the (3S, 4S, 5R) diastereomer (D-FBP) is obtained. Therefore, the chirality in the 3- and 4-positions is induced by the chirality of the enzyme composed of L-amino acid residues. D-Glucose-6-phosphate (D-G6P), which is generated from D-FBP in the gluconeogenesis pathway, produces D-ribose-5-phosphate (D-R5P) in the pentose phosphate pathway. D-R5P is converted to PRPP (5-phosphoribosyl-alpha-pyrophosphate), which is used for the de novo synthesis of nucleotides. Ribonucleic acid (RNA) uses the nucleotides as building blocks. The configurations of the 4R-carbon and of the 3S-carbon are retained. The stereochemical structure of RNA is based on 3S as well as 4R (D). The consideration above suggests that aldolase is a key enzyme that determines the 3S configuration in D-R5P. It is thus a chirality intersection between amino acids and sugars, because the sugar chirality is determined by the chiral environment of an L-amino acid protein, aldolase, to produce D-FBP.

リンク情報
DOI
https://doi.org/10.1007/s11084-015-9415-8
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000355820100018&DestApp=WOS_CPL
URL
https://link.springer.com/article/10.1007/s11084-015-9415-8
ID情報
  • DOI : 10.1007/s11084-015-9415-8
  • ISSN : 0169-6149
  • eISSN : 1573-0875
  • Web of Science ID : WOS:000355820100018

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