Enzymatic Aspects of Isoprenoid Chain Elongation

Ogura, Kyozo; Koyama, Tanetoshi

doi:10.1021/cr9600464

Cited by 326 publications

(285 citation statements)

References 108 publications

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“…Stabilization of oxocarbenium ion-like transition states by cation-p interactions could therefore be a common theme of catalysis by the members of this family. Several other enzymes [10,[37][38][39][40][41], among them glycosyltransferases [8,10] that show significant mechanistic analogy to glycoside hydrolases [42], have been proposed to stabilize (partial) positive charges in intermediates or transition states of their reaction, by up to 4 kcal/mol [37], with the help of p bonding interactions.…”

Section: Discussionmentioning

confidence: 99%

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe⁵² → Ala and Phe⁵² → Asn mutants

2011

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a b s t r a c tMutants of Leuconostoc mesenteroides sucrose phosphorylase having active-site Phe 52 replaced by Ala (F52A) or Asn (F52N) were characterized by free energy profile analysis for catalytic glucosyl transfer from sucrose to phosphate. Despite large destabilization (P3.5 kcal/mol) of the transition states for enzyme glucosylation and deglucosylation in both mutants as compared to wild-type, the relative stability of the glucosyl enzyme intermediate was weakly affected by substitution of Phe 52 . In reverse reaction where fructose becomes glucocylated, ''error hydrolysis'' was the preponderant path of breakdown of the covalent intermediate of F52A and F52N. It is proposed, therefore, that Phe 52 facilitates reaction of the phosphorylase through (1) positioning of the transferred glucosyl moiety at the catalytic subsite and (2) strong cation-p stabilization of the oxocarbenium ion-like transition states flanking the covalent enzyme intermediate.

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Section: Discussionmentioning

confidence: 99%

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe⁵² → Ala and Phe⁵² → Asn mutants

2011

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“…This system has been used before to demonstrate the function of putative GGPP synthases from Arabidopsis (Zhu et al 1997), sunXower (Helianthus annuus) (Oh et al 2000) makandi (Coleus forskohlii) (Engprasert et al 2004), human and mouse (Mus musculus) (Kainou et al 1999). While GGPP synthase, FPP synthase and most GPP synthases are functional as homodimers (Ogura and Koyama 1998), the GPP synthases from mint and snapdragon are functional as heterodimers (Burke et al 1999;Tholl et al 2004). In the phylogenetic tree ( Fig.…”

Section: Leggps1 Is Not a Typical Ja-or Sa-responsive Genementioning

confidence: 99%

Induction of a leaf specific geranylgeranyl pyrophosphate synthase and emission of (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene in tomato are dependent on both jasmonic acid and salicylic acid signaling pathways

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Bouwmeester³

et al. 2006

Planta

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Two cDNAs encoding geranylgeranyl pyrophosphate (GGPP) synthases from tomato (Lycopersicon esculentum) have been cloned and functionally expressed in Escherichia coli. LeGGPS1 was predominantly expressed in leaf tissue and LeGGPS2 in ripening fruit and Xower tissue. LeGGPS1 expression was induced in leaves by spider mite (Tetranychus urticae)-feeding and mechanical wounding in wild type tomato but not in the jasmonic acid (JA)-response mutant def-1 and the salicylic acid (SA)-deWcient transgenic NahG line. Furthermore, LeGGPS1 expression could be induced in leaves of wild type tomato plants by JA-or methyl salicylate (MeSA)-treatment. In contrast, expression of LeGGPS2 was not induced in leaves by spider mite-feeding, wounding, JA-or MeSA-treatment. We show that emission of the GGPP-derived volatile terpenoid (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT) correlates with expression of LeGGPS1. An exception was MeSA-treatment, which resulted in induction of LeGGPS1 but not in emission of TMTT. We show that there is an additional layer of regulation, because geranyllinalool synthase, catalyzing the Wrst dedicated step in TMTT biosynthesis, was induced by JA but not by MeSA.

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“…This reaction is catalyzed by highly conserved prenyl transferases and the elongation stops at discrete chain lengths, depending on enzyme specificity (Ogura and Koyama, 1998). The final size of the isoprenyl product is determined by the bulk of the lateral groups of certain amino acyl residues located in a hydrophobic pocket in the enzyme, as evidenced by x-ray crystallography and kinetic studies of wild-type avian farnesyl diphosphate synthase (FPPS; EC 2.5.1.1 and EC 2.5.1.10) and mutated enzymes in which such amino acyl residues have been substituted (Tarshis et al, 1996).…”

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Maize cDNAs Expressed in Endosperm Encode Functional Farnesyl Diphosphate Synthase with Geranylgeranyl Diphosphate Synthase Activity

et al. 2006

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Isoprenoids are the most diverse and abundant group of natural products. In plants, farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP) are precursors to many isoprenoids having essential functions. Terpenoids and sterols are derived from FPP, whereas gibberellins, carotenoids, casbenes, taxenes, and others originate from GGPP. The corresponding synthases (FPP synthase [FPPS] and GGPP synthase [GGPPS]) catalyze, respectively, the addition of two and three isopentenyl diphosphate molecules to dimethylallyl diphosphate. Maize (Zea mays L. cv B73) endosperm cDNAs encoding isoprenoid synthases were isolated by functional complementation of Escherichia coli cells carrying a bacterial gene cluster encoding all pathway enzymes needed for carotenoid biosynthesis, except for GGPPS. This approach indicated that the maize gene products were functional GGPPS enzymes. Yet, the predicted enzyme sequences revealed FPPS motifs and homology with FPPS enzymes. In vitro assays demonstrated that indeed these maize enzymes produced both FPP and GGPP and that the N-terminal sequence affected the ratio of FPP to GGPP. Their functionality in E. coli demonstrated that these maize enzymes can be coupled with a metabolon to provide isoprenoid substrates for pathway use, and suggests that enzyme bifunctionality can be harnessed. The maize cDNAs are encoded by a small gene family whose transcripts are prevalent in endosperm beginning mid development. These maize cDNAs will be valuable tools for assessing the critical structural properties determining prenyl transferase specificity and in metabolic engineering of isoprenoid pathways, especially in cereal crops.

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Enzymatic Aspects of Isoprenoid Chain Elongation

Cited by 326 publications

References 108 publications

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe⁵² → Ala and Phe⁵² → Asn mutants

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe⁵² → Ala and Phe⁵² → Asn mutants

Induction of a leaf specific geranylgeranyl pyrophosphate synthase and emission of (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene in tomato are dependent on both jasmonic acid and salicylic acid signaling pathways

Maize cDNAs Expressed in Endosperm Encode Functional Farnesyl Diphosphate Synthase with Geranylgeranyl Diphosphate Synthase Activity

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Enzymatic Aspects of Isoprenoid Chain Elongation

Cited by 326 publications

References 108 publications

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe52 → Ala and Phe52 → Asn mutants

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe52 → Ala and Phe52 → Asn mutants

Induction of a leaf specific geranylgeranyl pyrophosphate synthase and emission of (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene in tomato are dependent on both jasmonic acid and salicylic acid signaling pathways

Maize cDNAs Expressed in Endosperm Encode Functional Farnesyl Diphosphate Synthase with Geranylgeranyl Diphosphate Synthase Activity

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Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe⁵² → Ala and Phe⁵² → Asn mutants

Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe⁵² → Ala and Phe⁵² → Asn mutants