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| - | {{STRUCTURE_1mc4| PDB=1mc4 | SIZE=400| SCENE=Aspartate-semialdehyde_dehydrogenase/Cv/1 |right|CAPTION=Aspartate-semialdehyde dehydrogenase, [[1mc4]] }}
| + | <StructureSection load='1mb4' size='350' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene='45/452498/Cv/2'> |
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| | + | == Function == |
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| | '''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+. | | '''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+. |
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| - | == 3D Structures of Aspartate-semialdehyde dehydrogenase == | + | == Structural highlights == |
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| + | 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> |
| - | {{#tree:id=OrganizedByTopic|openlevels=0|
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| - | *Aspartate-semialdehyde dehydrogenase
| + | == 3D Structures of Aspartate-semialdehyde dehydrogenase == |
| - | | + | [[Aspartate-semialdehyde dehydrogenase 3D structures]] |
| - | **[[2qz9]], [[1mc4]] – VcASADH II – ''Vibrio cholerae''<br />
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| - | **[[2yv3]] – ASADH – ''Thermus thermiphilus''<br />
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| - | **[[1t4d]], [[1t4b]], [[1brm]] - EcASADH β - ''Escherichia coli''<br />
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| - | **[[1pu2]], [[1oza]], [[1pr3]], [[1ps8]] - HiASADH (mutant) – ''Haemophilus influenzae''<br />
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| - | **[[1nwc]] – HiASADH<br />
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| - | **[[1nwh]] – HiASADH reaction intermediate<br />
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| - | **[[2gyy]] – SpASADH – ''Streptococcus pneumonia''<br />
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| - | **[[3uw3]] - ASADH – ''Burkholderia thailandensis''
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| - | | + | |
| - | *ASADH binary complex
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| - | **[[2r00]] - VcASADH II + ASA<br />
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| - | **[[3llg]], [[3vos]] – MtASADH + glycerol+ anion – ''Mycobacterium tuberculosis''<br />
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| - | **[[3hsk]] – ASADH + NADP – ''Candida albicans''<br />
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| - | **[[1ys4]] - ASADH + NADP – ''Methanocaldococcus jannaschii''<br />
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| - | **[[1nx6]] - HiASADH reaction intermediate +Pi<br />
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| - | **[[1ta4]] - HiASADH + As<br />
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| - | **[[1tb4]] - HiASADH + IO4<br />
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| - | **[[1q2x]] - HiASADH (mutant) + ASA<br />
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| - | **[[2gz1]] - SpASADH + NADP<br />
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| - | **[[2gz2]] - SpASADH + ADP<br />
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| - | **[[3pyl]] - SpASADH + diaminopropionate<br />
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| - | **[[3q0e]] - VcASADH + cysteine sulfoxide<br />
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| - | **[[3q1l]] - SpASADH + cysteamine<br />
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| - | **[[3tz6]] - MtASADH + cysteine
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| - | *ASADH ternary complex
| + | </StructureSection> |
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| - | **[[1pqu]] - HiASADH (mutant) + NADP + cacodylate + substrate analog<br />
| + | == References == |
| - | **[[1pqp]] - HiASADH (mutant) + ASA + Pi<br />
| + | <references/> |
| - | **[[1gl3]] - EcASADH β + NADP + substrate analog<br />
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| - | **[[1mb4]] - VcASADH + NADP + substrate analog<br />
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| - | **[[3pzr]] - VcASADH + NADP + carbamoyl-cysteine <br />
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| - | **[[2gz3]] - SpASADH + NADP + ASA<br />
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| - | **[[3pwk]], [[3pws]] - SpASADH + NADP + aminoadipate<br />
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| - | **[[3pyx]] - SpASADH + NADP + aminoterephthalate <br />
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| - | **[[3pzb]] - SpASADH + NADP + diaminopropionate<br />
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| - | **[[3q11]], [[4r3n]], [[4r3w]], [[4r41]], [[4r4j]], [[4r51]], [[4r54]], [[4r5h]] - SpASADH + NADP + inhibitor<br />
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| - | **[[4r5m]] - VcASADH I + NADP + inhibitor<br />
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| - | }}
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