Acetyl-CoA carboxylase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Acetyl-CoA carboxylase''' (ACC) catalyzes the irreversible carboxylation of acetyl-CoA to malonyl-CoA. | + | '''Acetyl-CoA carboxylase''' (ACC) catalyzes the irreversible carboxylation of <scene name='43/430893/Cv/2'>acetyl-CoA</scene> to <scene name='49/492046/Cv/7'>malonyl-CoA</scene>. Malonyl-CoA is a building block in in the biosynthesis of fatty acids. ACC is biotin- and ATP-dependent enzyme. In mammals, 2 forms of ACC exist. ACC1 and ACC2 differ in their tissue distribution and function. See also [[3-Hydroxypropionate bicycle]]. |
== Structural highlights == | == Structural highlights == | ||
ACC is a multi-subunit enzyme in prokaryotes and plants. Each subunit catalyzes different reaction. These are – '''biotin carboxylase''' (BC) which carboxylates the biotin prosthetic group, '''biotin carboxyl carrier protein''' (BCCP) which is linked covalently to biotin and '''carboxyltransferase''' (CT) which transfers the carboxyl group from biotin to acetyl-CoA. In eukaryotes these functions are performed by a single polypeptide chain. The biotin moiety is located in the beta turn connecting the N and C halves of BCCP. <scene name='49/492046/Cv/6'>E.coli biotin carboxylase complex with biotin</scene> ([[1bdo]]) is shown. <ref>PMID:8747466</ref> Water molecules shown as red spheres. | ACC is a multi-subunit enzyme in prokaryotes and plants. Each subunit catalyzes different reaction. These are – '''biotin carboxylase''' (BC) which carboxylates the biotin prosthetic group, '''biotin carboxyl carrier protein''' (BCCP) which is linked covalently to biotin and '''carboxyltransferase''' (CT) which transfers the carboxyl group from biotin to acetyl-CoA. In eukaryotes these functions are performed by a single polypeptide chain. The biotin moiety is located in the beta turn connecting the N and C halves of BCCP. <scene name='49/492046/Cv/6'>E.coli biotin carboxylase complex with biotin</scene> ([[1bdo]]) is shown. <ref>PMID:8747466</ref> Water molecules shown as red spheres. | ||
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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of acetyl-CoA carboxylase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *Acetyl-CoA carboxylase | ||
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| - | **[[6g2d]] – hACC1 – human – Cryo EM<br /> | ||
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| - | *Biotin carboxyl carrier protein (BCCP) domain | ||
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| - | **[[1bnc]], [[1dv1]] - EcBCCP – ''Escherichia coli''<br /> | ||
| - | **[[2gps]], [[2gpw]], [[3g8d]] - EcBCCP (mutant)<br /> | ||
| - | **[[1a6x]], [[3bdo]] – EcBCCP biotinyl domain – NMR<BR /> | ||
| - | **[[2dn8]] – hBCCP2 residues 8-94 - NMR<BR /> | ||
| - | **[[2kcc]] - hBCCP2 residues 891-964 – NMR<br /> | ||
| - | **[[2hjw]] - hBCCP2 BC domain<br /> | ||
| - | **[[3glk]], [[3jrw]] – hBCCP2<br /> | ||
| - | **[[4hq6]] – hBCCP2 (mutant)<br /> | ||
| - | **[[2yl2]] – hBCCP1<br /> | ||
| - | **[[2c00]] – BCCP – ''Pseudomonas aeruginosa''<br /> | ||
| - | **[[1w93]] – yBCCP – yeast <br /> | ||
| - | **[[2vpq]] – SaBCCP – ''Staphylococcus aureus''<br /> | ||
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| - | * Biotin carboxyl carrier protein (BCCP) subunit complex | ||
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| - | **[[1bdo]] - EcBCCP + biotin <br /> | ||
| - | **[[2bdo]] - EcBCCP + biotin – NMR<br /> | ||
| - | **[[1w96]] – yBCCP + soraphen <br /> | ||
| - | **[[3gid]], [[3jrx]] – hBCCP2 + soraphen <br /> | ||
| - | **[[2j9g]] – EcBCCP + AMPPNP + ADP<br /> | ||
| - | **[[1dv2]] – EcBCCP (mutant) + ATP<br /> | ||
| - | **[[3rup]] - EcBCCP + Ca + ADP<br /> | ||
| - | **[[3rv3]] - EcBCCP + Mg + ADP<br /> | ||
| - | **[[3rv4]] - EcBCCP + bicarbonate + Mg-ADP<br /> | ||
| - | **[[3g8c]] - EcBCCP + biotin + bicarbonate + Mg + ADP<br /> | ||
| - | **[[2vr1]] - EcBCCP + ATP analog<br /> | ||
| - | **[[2vpq]] - SaBCCP + AMPPNP <br /> | ||
| - | **[[2vqd]] - SaBCCP + AMPCP<br /> | ||
| - | **[[3ouz]] - CjBCCP + ADP – Campylobacter jejuni<br /> | ||
| - | **[[3ouu]] - CjBCCP + b-g-ATP<br /> | ||
| - | **[[4hr7]] – EcBCCP + biotin carboxyl carrier protein<br /> | ||
| - | **[[4mv1]] – HiBCCP + Pi + ADP – Haemophilus influenzae<br /> | ||
| - | **[[4mv3]] – HiBCCP + bicarbonate + AMPCP <br /> | ||
| - | **[[4mv4]] – HiBCCP + Mg + AMPCP <br /> | ||
| - | **[[4mv8]] – HiBCCP + Pi + AMPCP <br /> | ||
| - | **[[4mv9]] – HiBCCP + bicarbonate <br /> | ||
| - | **[[4mv6]], [[4mv7]] – HiBCCP + phosphoacetamide <br /> | ||
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| - | * Biotin carboxyl carrier protein (BCCP) subunit complex with inhibitors | ||
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| - | **[[2v58]], [[2v59]], [[2v5a]] - EcBCCP + inhibitor<br /> | ||
| - | **[[2w6m]], [[2w6n]], [[2w6o]], [[2w6p]], [[2w6q]], [[2w6z]], [[2w70]], [[2w71]] - EcBCCP + fragment-based inhibitor<br /> | ||
| - | **[[3jzf]], [[3jzi]] - EcBCCP + benzimidazole inhibitor<br /> | ||
| - | **[[1w96]] – yBCCP + soraphen <br /> | ||
| - | **[[3ff6]], [[5kkn]] – hBCCP2 + inhibitor <br /> | ||
| - | **[[3gid]], [[3jrx]] – hBCCP2 + soraphen <br /> | ||
| - | **[[3pgq]] - CjBCCP + pinoxaden | ||
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| - | *Carboxyltransferase (CT) domain | ||
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| - | **[[1uyt]], [[5i6e]] - yCT <BR /> | ||
| - | **[[1uyv]] - yCT (mutant) <BR /> | ||
| - | **[[2f9i]] - SaCT <BR /> | ||
| - | **[[2f9y]] - EcCT <BR /> | ||
| - | **[[5kdr]] - SaCT + moiramide <BR /> | ||
| - | **[[1od2]] - yCT + adenine + acetyl CoA <BR /> | ||
| - | **[[1od4]] - yCT + adenine<BR /> | ||
| - | **[[1uyr]], [[1uys]], [[1w2x]], [[3k8x]], [[3h0j]], [[3h0s]], [[3h0q]], [[3pgq]], [[3tv5]], [[3tvu]], [[3tvw]], [[3tz3]], [[4wyo]], [[4wz8]], [[5ctb]], [[5ctc]], [[5cte]] - yCT + inhibitor<BR /> | ||
| - | **[[2x24]] - CT + inhibitor – bovine<br /> | ||
| - | **[[3tdc]] - hCT2 residues 921-1676<br /> | ||
| - | **[[4asi]] - hCT1 residues 1493-2260<br /> | ||
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| - | *AC domains | ||
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| - | **[[5cs0]] – yAC AC1-AC2<br /> | ||
| - | **[[5cs4]], [[5trc]] – yAC AC3-AC5<br /> | ||
| - | **[[5csa]] – yAC AC1-AC5+BCCP<br /> | ||
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| - | *BT-CD domains | ||
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| - | **[[5i87]] – hAC <br /> | ||
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| - | *Full ACC | ||
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| - | **[[5csk]], [[5csl]] – yAC <br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Athappilly FK, Hendrickson WA. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure. 1995 Dec 15;3(12):1407-19. PMID:8747466
