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・ MALAT1-associated small cytoplasmic RNA
・ Malatang
・ Malataverne
・ Malate Catholic School
・ Malate Church
・ Malate dehydrogenase
・ Malate dehydrogenase (decarboxylating)
・ Malate dehydrogenase (disambiguation)
・ Malate dehydrogenase (NAD(P)+)
・ Malate dehydrogenase (NADP+)
・ Malate dehydrogenase (oxaloacetate-decarboxylating)
・ Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
・ Malate dehydrogenase (quinone)
・ Malate dehydrogenase 2
・ Malate oxidase
Malate synthase
・ Malate, Manila
・ Malate-aspartate shuttle
・ Malateh
・ Malatesta
・ Malatesta (film)
・ Malatesta (Rome Metro)
・ Malatesta da Verucchio
・ Malatesta II Baglioni
・ Malatesta II Malatesta
・ Malatesta IV Malatesta
・ Malatesta Malatesta
・ Malatesta Novello
・ Malatesta Ungaro
・ Malatestiana Library


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Malate synthase : ウィキペディア英語版
Malate synthase

In enzymology, a malate synthase () is an enzyme that catalyzes the chemical reaction
:acetyl-CoA + H2O + glyoxylate \rightleftharpoons (S)-malate + CoA
The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include L-malate glyoxylate-lyase (CoA-acetylating), glyoxylate transacetylase, glyoxylate transacetase, glyoxylic transacetase, malate condensing enzyme, malate synthetase, malic synthetase, and malic-condensing enzyme. This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.
==Structure and Isoforms==
Malate synthases fall into two major families, isoforms A and G. Isoform G is monomeric with a size of ~80-kD and found exclusively in bacteria. Isoform A is about ~65 kD per subunit, and can form homomultimers in eukaryotes. This enzyme contains a central TIM barrel sandwiched between an N-terminal alpha-helical clasp and an alpha/beta domain stemming from two insertions into the TIM barrel sequence. Then the enzyme ends with a C-terminal five-helix plug. The active site, where the acetyl-CoA and glyoxylate bind to the enzyme, lie between the TIM barrel and C-terminal plug. Upon binding, the acetyl-CoA molecule forms a J-shape inserted into the binding pocket, by an intramolecular hydrogen bond between N7 of the adenine ring and a hydroxyl group on the pantetheine tail.〔 In addition, a critical magnesium ion within the active site coordinates with glyoxylate, glutamic acid 427, aspartic acid 455, and two water molecules.〔 The amino acids interacting with acetyl CoA upon binding are highly conserved.〔 Sequence identity is high within each class of isoforms, but between both classes sequence identity drops to about 15%. The alpha/beta domain, which has no apparent function, is not seen in isoform A.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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