The Structure and Computational Analysis of Mycobacterium tuberculosis Protein CitE Suggest a Novel Enzymatic Function

Goulding, Celia W.; Bowers, Peter M.; Segelke, Brent W.; Lekin, T.; Kim, Chang-Yub; Terwilliger, Thomas C.; Eisenberg, David

doi:10.1016/j.jmb.2006.09.086

Cited by 36 publications

(51 citation statements)

References 26 publications

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“…They differ mainly by the presence of an additional domain in the G isoform that may have a regulatory function (25). The crystal structures of malate synthase G (MSG) from Mycobacterium tuberculosis and E. coli, of malate synthase A (MSA) from E. coli and Bacillus anthracis, and of a malyl-CoA lyase-like protein with unknown function from M. tuberculosis have been determined (2,3,15,20,25,29). They all contain a conserved ␣ 8 ␤ 8 TIM (triose phosphate isomerase fold) barrel that harbors the active site.…”

Section: Resultsmentioning

confidence: 99%

The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3 S )-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3 S )- Malyl-CoA Thioesterase

et al. 2010

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Section: Resultsmentioning

confidence: 99%

The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3 S )-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3 S )- Malyl-CoA Thioesterase

et al. 2010

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“…Homology searching revealed that TtmO has high homology to the citryl-CoA lyase (CitE), which converts citryl-CoA to acetyl-CoA and oxaloactate in Mycobacterium tuberculosis (41). Thus, TtmO is a candidate to catalyze the aldol type condensation step.…”

Section: Genes Encoding Modular Polyketide Synthases For the Biosynthmentioning

confidence: 99%

Characterization of the Tautomycin Biosynthetic Gene Cluster from Streptomyces spiroverticillatus Unveiling New Insights into Dialkylmaleic Anhydride and Polyketide Biosynthesis

Rajski

et al. 2008

Journal of Biological Chemistry

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Tautomycin (TTM) is a highly potent and specific protein phosphatase inhibitor isolated from Streptomyces spiroverticillatus. The biological activity of TTM makes it an important lead for drug discovery, whereas its spiroketal-containing polyketide chain and rare dialkylmaleic anhydride moiety draw attention to novel biosynthetic chemistries responsible for its production. To elucidate the biosynthetic machinery associated with these novel molecular features, the ttm biosynthetic gene cluster from S. spiroverticillatus was isolated and characterized, and its involvement in TTM biosynthesis was confirmed by gene inactivation and complementation experiments. The ttm cluster was localized to a 86-kb DNA region, consisting of 20 open reading frames that encode three modular type I polyketide synthases (TtmHIJ), one type II thioesterase (TtmT), five proteins for methoxymalonyl-S-acyl carrier protein biosynthesis (Ttm-ABCDE), eight proteins for dialkylmaleic anhydride biosynthesis and regulation (TtmKLMNOPRS), as well as two additional regulatory proteins (TtmF and TtmQ) and one tailoring enzyme (TtmG). A model for TTM biosynthesis is proposed based on functional assignments from sequence analysis, which agrees well with previous feeding experiments, and has been further supported by in vivo gene inactivation experiments. These findings set the stage to fully investigate TTM biosynthesis and to biosynthetically engineer new TTM analogs.

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“…This structure was solved by a structural genomics consortium and is unpublished, although the Mycobacterium tuberculosis structure has recently been communicated. 24 HpcH, DDGA and citrate lyase all catalyse very similar reactions on similar substrates; namely a retro-aldol reaction in which a carbon-carbon bond is broken. Hence the structural homology is understandable.…”

Section: Related Structuresmentioning

confidence: 99%

Structure and Mechanism of HpcH: A Metal Ion Dependent Class II Aldolase from the Homoprotocatechuate Degradation Pathway of Escherichia coli

Rea

Fülöp

Bugg

et al. 2007

Journal of Molecular Biology

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The Structure and Computational Analysis of Mycobacterium tuberculosis Protein CitE Suggest a Novel Enzymatic Function

Cited by 36 publications

References 26 publications

The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3 S )-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3 S )- Malyl-CoA Thioesterase

The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3 S )-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3 S )- Malyl-CoA Thioesterase

Characterization of the Tautomycin Biosynthetic Gene Cluster from Streptomyces spiroverticillatus Unveiling New Insights into Dialkylmaleic Anhydride and Polyketide Biosynthesis

Structure and Mechanism of HpcH: A Metal Ion Dependent Class II Aldolase from the Homoprotocatechuate Degradation Pathway of Escherichia coli

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