Aspartate-semialdehyde dehydrogenase: Difference between revisions

Latest revision as of 14:31, 20 March 2019

Function

Aspartate-semialdehyde dehydrogenase (ASADH) is an enzyme which is part of the biosynthesis of amino acids in bacteria, plants and fungi. It catalyzes the conversion of L-aspartate 4-semialdehyde (ASA) + phosphate + NADP to L-4-aspartyl phosphate + NADPH + H+.

Structural highlights

ASADH contains 2 domains. The N terminal domain contains the and the . The active site contains a (C134 in Vibrio Cholerae) which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts. ^[1]

3D Structures of Aspartate-semialdehyde dehydrogenase

Aspartate-semialdehyde dehydrogenase 3D structures

Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code 1mb4)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Blanco J, Moore RA, Kabaleeswaran V, Viola RE. A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. Protein Sci. 2003 Jan;12(1):27-33. PMID:12493825

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Alexander Berchansky, Michal Harel

[1] Blanco J, Moore RA, Kabaleeswaran V, Viola RE. A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. Protein Sci. 2003 Jan;12(1):27-33. PMID:12493825

[1]

@@ Line 7: / Line 7: @@
 == Structural highlights ==
-ASADH contains 2 domains.  The N terminal domain contains the <scene name='45/452498/Cv/3'>active site</scene> and the <scene name='45/452498/Cv/4'>NADP-binding site</scene>.  The active site contains a <scene name='45/452498/Cv/5'>cysteine residue</scene> (C134 in ''Vibrio Cholerae'') which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref>
+ASADH contains 2 domains.  The N terminal domain contains the <scene name='45/452498/Cv/7'>active site</scene> and the <scene name='45/452498/Cv/9'>NADP-binding site</scene>.  The active site contains a <scene name='45/452498/Cv/10'>cysteine residue</scene> (C134 in ''Vibrio Cholerae'') which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref>
-</StructureSection>
 == 3D Structures of Aspartate-semialdehyde dehydrogenase ==
+[[Aspartate-semialdehyde dehydrogenase 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+</StructureSection>
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Aspartate-semialdehyde dehydrogenase
-**[[2qz9]], [[1mc4]] – VcASADH II – ''Vibrio cholerae''<br />
-**[[2yv3]] – ASADH – ''Thermus thermiphilus''<br />
-**[[1t4d]], [[1t4b]], [[1brm]] - EcASADH β - ''Escherichia coli''<br />
-**[[1pu2]], [[1oza]], [[1pr3]], [[1ps8]] - HiASADH (mutant) – ''Haemophilus influenzae''<br />
-**[[1nwc]] – HiASADH<br />
-**[[1nwh]] – HiASADH reaction intermediate<br />
-**[[2gyy]] – SpASADH – ''Streptococcus pneumonia''<br />
-**[[3uw3]] - ASADH – ''Burkholderia thailandensis''
-**[[4woj]] – ASADH – ''Francisella tularensis''<br />
-**[[4zhs]] – TrASADH – ''Trichophyton rubrum''<br />
-**[[5cef]] – ASADH – ''Cryptococcus neoformans''<br />
-**[[5jw6]] – ASADH – ''Neosartorya fumigata''<br />
-**[[6bac]] - ASADH – ''Neisseria gonorrhoeae''<br />
-*ASADH binary complex
-**[[2r00]] - VcASADH II + ASA<br />
-**[[3vos]] – MtASADH + glycerol+ anion – ''Mycobacterium tuberculosis''<br />
-**[[3hsk]] – ASADH + NADP – ''Candida albicans''<br />
-**[[1ys4]] - ASADH + NADP – ''Methanocaldococcus jannaschii''<br />
-**[[4zic]] – TrASADH + NADP<br />
-**[[5bnt]] – ASADH + NADP – ''Pseudomonas aeruginosa''<br />
-**[[1nx6]] - HiASADH reaction intermediate +Pi<br />
-**[[1ta4]] - HiASADH + As<br />
-**[[1tb4]] - HiASADH + IO4<br />
-**[[1q2x]] - HiASADH (mutant) + ASA<br />
-**[[2gz1]] - SpASADH + NADP<br />
-**[[2gz2]] - SpASADH + ADP<br />
-**[[3pyl]] - SpASADH + diaminopropionate<br />
-**[[3q0e]] - VcASADH + cysteine sulfoxide<br />
-**[[3q1l]] - SpASADH + cysteamine<br />
-**[[3tz6]] - MtASADH + cysteine
-*ASADH ternary complex
-**[[1pqu]] - HiASADH (mutant) + NADP + cacodylate + substrate analog<br />
-**[[1pqp]] - HiASADH (mutant) + ASA + Pi<br />
-**[[1gl3]] - EcASADH β + NADP + substrate analog<br />
-**[[1mb4]] - VcASADH + NADP + substrate analog<br />
-**[[3pzr]] - VcASADH + NADP + carbamoyl-cysteine <br />
-**[[2gz3]] - SpASADH + NADP + ASA<br />
-**[[3pwk]], [[3pws]] - SpASADH + NADP + aminoadipate<br />
-**[[3pyx]] - SpASADH + NADP + aminoterephthalate <br />
-**[[3pzb]] - SpASADH + NADP + diaminopropionate<br />
-**[[3q11]], [[4r3n]], [[4r3w]], [[4r41]], [[4r4j]], [[4r51]], [[4r54]], [[4r5h]] - SpASADH + NADP + inhibitor<br />
-**[[4r5m]] - VcASADH I + NADP + inhibitor<br />
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]