Malate synthase: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(16 intermediate revisions by 4 users not shown)
Line 1: Line 1:
<StructureSection load='1n8w' size='350' side='right' caption='Structure of malate synthase complex with CoA, glyoxylate, sulfate and Mg+2 ion (green) (PDB entry [[1n8w]])' scene=''>
<StructureSection load='' size='350' side='right' caption='Structure of malate synthase G complex with CoA, malate, Hepes and Mg+2 ion (green) (PDB entry [[2gq3]])' scene='57/573146/Cv/1'>
   
== Function ==   
'''Malate synthase''' (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to (S)-malate and CoA.  MS participates in pyruvate, glyoxylate and dicarboxylate metabolism.  There are 2 isozymes of MS.  '''MS G''' is formed during growth on glycolate and '''MS A''' which metabolizes glyoxylate formed in the dissimilation of acetate.
'''Malate synthase''' (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to [[R/S nomenclature|(S)]]-malate and CoA.  MS participates in pyruvate, glyoxylate and dicarboxylate metabolism.  There are 2 isozymes of MS.  '''MS G''' is formed during growth on glycolate<ref>PMID:12930982</ref> and '''MS A''' which metabolizes glyoxylate formed in the dissimilation of acetate.


==3d structures of malate synthase==
See also: [[Glyoxylate cycle]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
== Structural highlights ==
<scene name='57/573146/Cv/8'>MS active site pocket is situated between the TIM barrel and the C-terminal</scene>.  The ternary complex contains malate, acetyl-CoA and Mg+2 ion<ref>PMID:16877713</ref>.


===Malate synthase ===
<scene name='57/573146/Cv/9'>Malate/Mg+2 ion binding site</scene>. Water molecules  are shown as red spheres.


[[1y8b]], [[2jqx]] – EcMS G (mutant) – ''Escherichia coli'' - NMR<br />
<scene name='57/573146/Cv/10'>Acetyl-CoA binding site</scene>.
[[3cuz]], [[3cv1]] – EcMS A<br />
[[4ex4]] – MS G + Mg – ''Mycobacterium leprae''<br />
[[3cux]] – MS + Mg – ''Bacillus anthracis''<br />


===Malate synthase binary complex===
==3d structures of malate synthase==
 
[[Malate synthase 3D structures]]
[[1d8c]] – EcMS G (mutant) + glyoxylate + Mg <br />
[[3cv2]] – EcMS A + oxalate + Mg <br />
[[1n8i]] – MtMS G + glyoxylate + Mg – ''Mycobacterium tuberculosis''<br />
[[3oyx]], [[3pug]] – HvMS + glyoxylate + Mg – ''Haloferax volcanii''<br />
[[3s9i]], [[3s9z]], [[3sad]], [[3saz]], [[3sb0]] – MtMS G (mutant) + inhibitor + Mg <br />
 
===Malate synthase ternary complex===


[[1p7t]] – EcMS G (mutant) + pyruvate + Mg + acetyl-CoA<br />
</StructureSection>
[[3oyz]] – HvMS + pyruvate + Mg + acetyl-CoA<br />
[[1n8w]] – MtMS G + glyoxylate + Mg + CoA<br />
[[2gq3]] – MtMS G + malate + Mg + CoA<br />


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:03, 11 January 2023

Function

Malate synthase (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to (S)-malate and CoA. MS participates in pyruvate, glyoxylate and dicarboxylate metabolism. There are 2 isozymes of MS. MS G is formed during growth on glycolate[1] and MS A which metabolizes glyoxylate formed in the dissimilation of acetate.

See also: Glyoxylate cycle

Structural highlights

. The ternary complex contains malate, acetyl-CoA and Mg+2 ion[2].

. Water molecules are shown as red spheres.

.

3d structures of malate synthase

Malate synthase 3D structures


Structure of malate synthase G complex with CoA, malate, Hepes and Mg+2 ion (green) (PDB entry 2gq3)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. PMID:12930982
  2. Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713 doi:15/8/2002

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Karsten Theis