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Literature summary for 6.4.1.5 extracted from

  • Jurado, A.; Huang, C.; Zhang, X.; Zhou, Z.; Tong, L.
    Structure and substrate selectivity of the 750-kDa alpha6beta6 holoenzyme of geranyl-CoA carboxylase (2015), Nat. Commun., 6, 8986 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the 750-kDa alpha6beta6 holoenzyme and comparison with 3-methylcrotonyl-CoA carboxylase, EC 6.4.1.4. Structural differences in the active site region of both enzymes explain their distinct substrate preferences and support two distinct lineages of biotin-dependent acyl-CoA carboxylases, one carboxylating the alpha carbon of a saturated organic acid and the other carboxylating the gamma carbon of an alpha-beta unsaturated acid. A glycine residue in geranyl-CoA carboxylase is replaced by phenylalanine in 3-methylcrotonyl-CoA carboxylase, which blocks access by the larger geranyl-CoA substrate Pseudomonas fluorescens
structure of the hexamer of the beta-subunit, to 2.4 A resolution Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HZV9 beta subunit AtuC
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Pseudomonas aeruginosa DSM 22644 Q9HZV9 beta subunit AtuC
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Pseudomonas fluorescens
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Synonyms

Synonyms Comment Organism
AtuC
-
 Pseudomonas fluorescens
AtuC
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 Pseudomonas aeruginosa