Evidence for distinct 3-methylcrotonyl-CoA and geranyl-CoA carboxylases in Pseudomonas citronellolis

Hector, Mina L.; Fall, Ray

doi:10.1016/0006-291x(76)90894-9

Cited by 12 publications

(7 citation statements)

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“…Maximal enzyme activity occurs at 35OC in the case of pea leaf MCase and at 38OC in the case of the potato tuber enzyme (Table 111). These optimum temperatures were in the same order as those reported for mammalian and bacterial MCase (Lau et al, 1980;Schiele and Lynen, 1981); however, plant MCase, unlike Pseudomonas citronellolis MCase (Hector and Fall, 1976), was not inactivated, even partially, upon heating to 5OoC for 1 min.…”

Section: Biochemical Propertiessupporting

confidence: 61%

Purification and Characterization of 3-Methylcrotonyl-Coenzyme A Carboxylase from Higher Plant Mitochondria

et al. 1993

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Section: Biochemical Propertiessupporting

confidence: 61%

Purification and Characterization of 3-Methylcrotonyl-Coenzyme A Carboxylase from Higher Plant Mitochondria

et al. 1993

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“…Geranyl-CoA carboxylase (GCC) activity was first purified from a Pseudomonas organism grown with either the related acyclic monoterpenoid citronellol 4 or geranic acid 5 6 7 as the sole carbon source. GCC also possesses 3-methylcrotonyl-CoA carboxylase (MCC) activity 5 6 8 , and 3-methylcrotonyl-CoA is an intermediate in the complete catabolism of citronellol and geranic acid ( Fig. 1a ).…”

mentioning

confidence: 99%

Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase

et al. 2015

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Geranyl-CoA carboxylase (GCC) is essential for the growth of Pseudomonas organisms with geranic acid as the sole carbon source. GCC has the same domain organization and shares strong sequence conservation with the related biotin-dependent carboxylases 3-methylcrotonyl-CoA carboxylase (MCC) and propionyl-CoA carboxylase (PCC). Here we report the crystal structure of the 750-kDa α6β6 holoenzyme of GCC, which is similar to MCC but strikingly different from PCC. The structures provide evidence in support of two distinct lineages of biotin-dependent acyl-CoA carboxylases, one carboxylating the α carbon of a saturated organic acid and the other carboxylating the γ carbon of an α-β unsaturated acid. Structural differences in the active site region of GCC and MCC explain their distinct substrate preferences. Especially, a glycine residue in GCC is replaced by phenylalanine in MCC, which blocks access by the larger geranyl-CoA substrate. Mutation of this residue in the two enzymes can change their substrate preferences.

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“…GCCase has been purified from P. citronellolis (2,6,7). The purified enzyme is composed of two nonidentical subunits, a biotin-containing subunit of 75 kDa and a nonbiotinylated subunit of 63 kDa (7).…”

mentioning

confidence: 99%

Geranoyl-CoA Carboxylase: A Novel Biotin-Containing Enzyme in Plants

Guan

Diez

Prasad

et al. 1999

Archives of Biochemistry and Biophysics

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Evidence for distinct 3-methylcrotonyl-CoA and geranyl-CoA carboxylases in Pseudomonas citronellolis

Cited by 12 publications

References 1 publication

Purification and Characterization of 3-Methylcrotonyl-Coenzyme A Carboxylase from Higher Plant Mitochondria

Purification and Characterization of 3-Methylcrotonyl-Coenzyme A Carboxylase from Higher Plant Mitochondria

Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase

Geranoyl-CoA Carboxylase: A Novel Biotin-Containing Enzyme in Plants

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