Jorge C. Escalante-Semerena

article

In Salmonella enterica, the pathogenicity island 2 (SPI‐2) regulator PagR regulates its own expression and the expression of a five‐gene operon that encodes transketolase C

Anastacia R. Parks, Regan D. McCormick, Jordan A. Byrne, Jorge C. Escalante‐Semerena

Molecular Microbiology > 120 > 4 > 575 - 586

The enteropathogen Salmonella enterica subsp. enterica sv. Typhimurium str. LT2 (hereafter S. Typhimurium) utilizes a cluster of genes encoded within the pathogenicity island 2 (SPI‐2) of its genome to proliferate inside macrophages. The expression of SPI‐2 is controlled by a complex network of transcriptional regulators and environmental cues, which now include a recently characterized DNA‐binding...

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Localization and interaction studies of the Salmonella enterica ethanolamine ammonia‐lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase

Flavia G. Costa, Jorge C. Escalante‐Semerena

Molecular Microbiology > 118 > 3 > 191 - 207

Some prokaryotes compartmentalize select metabolic capabilities. Salmonella enterica subspecies enterica serovar Typhimurium LT2 (hereafter S. Typhimurium) catabolizes ethanolamine (EA) within a proteinaceous compartment that we refer to as the ethanolamine utilization (Eut) metabolosome. EA catabolism is initiated by the adenosylcobalamin (AdoCbl)‐dependent ethanolamine ammonia‐lyase (EAL), which...

article

New AMP‐forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation

Rachel M. Burckhardt, Chelsey M. VanDrisse, Alex C. Tucker, Jorge C. Escalante‐Semerena

Molecular Microbiology > 113 > 1 > 253 - 269

In nature, organic acids are a commonly used source of carbon and energy. Many bacteria use AMP‐forming acid:CoA ligases to convert organic acids into their corresponding acyl‐CoA derivatives, which can then enter metabolism. The soil environment contains a broad diversity of organic acids, so it is not surprising that bacteria such as Streptomyces lividans can activate many of the available organic...

article

Staphylococcus aureus modulates the activity of acetyl‐Coenzyme A synthetase (Acs) by sirtuin‐dependent reversible lysine acetylation

Rachel M. Burckhardt, Brandi A. Buckner, Jorge C. Escalante‐Semerena

Molecular Microbiology > 112 > 2 > 588 - 604

Lysine acylation is a posttranslational modification used by cells of all domains of life to modulate cellular processes in response to metabolic stress. The paradigm for the role of lysine acylation in metabolism is the acetyl‐coenzyme A synthetase (Acs) enzyme. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging...

article

Rhodobacterales use a unique L‐threonine kinase for the assembly of the nucleotide loop of coenzyme B₁₂

Norbert K. Tavares, Chelsey M. VanDrisse, Jorge C. Escalante‐Semerena

Molecular Microbiology > 110 > 2 > 239 - 261

Several of the enzymes involved in the conversion of adenosylcobyric acid (AdoCby) to adenosylcobamide (AdoCba) are yet to be identified and characterized in some cobamide (Cba)‐producing prokaryotes. Using a bioinformatics approach, we identified the bluE gene (locus tag RSP_0788) of Rhodobacter sphaeroides 2.4.1 as a putative functional homolog of the L‐threonine kinase enzyme (PduX, EC 2.7.1.177)...

article

In Streptomyces lividans, acetyl‐CoA synthetase activity is controlled by O‐serine and N^ɛ‐lysine acetylation

Chelsey M. VanDrisse, Jorge C. Escalante‐Semerena

Molecular Microbiology > 107 > 4 > 577 - 594

Protein acetylation is a rapid mechanism for control of protein function. Acetyl‐CoA synthetase (AMP‐forming, Acs) is the paradigm for the control of metabolic enzymes by lysine acetylation. In many bacteria, type I or II protein acetyltransferases acetylate Acs, however, in actinomycetes type III protein acetyltransferases control the activity of Acs. We measured changes in the activity of the Streptomyces lividans...

article

A snapshot of evolution in action: emergence of new heme transport function derived from a coenzyme B₁₂ biosynthetic enzyme

Norbert K. Tavares, Jorge C. Escalante‐Semerena

Environmental Microbiology > 19 > 1 > 8 - 10

article

Salmonella enterica synthesizes 5,6‐dimethylbenzimidazolyl‐(DMB)‐α‐riboside. Why some Firmicutes do not require the canonical DMB activation system to synthesize adenosylcobalamin

Theodoric A. Mattes, Jorge C. Escalante‐Semerena

Molecular Microbiology > 103 > 2 > 269 - 281

5,6‐Dimethylbenzimidazolyl‐(DMB)‐α‐ribotide [α‐ribazole‐5′‐phosphate (α‐RP)] is an intermediate in the biosynthesis of adenosylcobalamin (AdoCbl) in many prokaryotes. In such microbes, α‐RP is synthesized by nicotinate mononucleotide (NaMN):DMB phosphoribosyltransferases (CobT in Salmonella enterica), in a reaction that is considered to be the canonical step for the activation of the base of the nucleotide...

chapter

Conversion of Cobinamide into Coenzyme B₁₂

Jorge C. Escalante-Semerena, Jesse D. Woodson, Nicole R. Buan, Carmen L. Zayas

Molecular Biology Intelligence Unit > Tetrapyrroles > 300-316

Cobamides are unique cyclic tetrapyrroles because their structures include an upper (Coβ) and a lower (Coα) axial ligand. The Coα and Coβ ligands are important for the interaction of the cobamide with enzymes, and for the chemistry of the reaction catalyzed by the enzyme. B₁₂ (5,6-dimethylbenzimidazolylcobamide, cobalamin) is the best-known cobamide, which in its vitamin form has a cyano...

article

The EutQ and EutP proteins are novel acetate kinases involved in ethanolamine catabolism: physiological implications for the function of the ethanolamine metabolosome in Salmonella enterica

Theodore C. Moore, Jorge C. Escalante‐Semerena

Molecular Microbiology > 99 > 3 > 497 - 511

Salmonella enterica catabolizes ethanolamine inside a compartment known as the metabolosome. The ethanolamine utilization (eut) operon of this bacterium encodes all functions needed for the assembly and function of this structure. To date, the roles of EutQ and EutP were not known. Herein we show that both proteins have acetate kinase activity and that EutQ is required during anoxic growth of S. enterica...

article

Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri

Kiyoung Park, Paola E. Mera, Jorge C. Escalante-Semerena, Thomas C. Brunold

JBIC Journal of Biological Inorganic Chemistry > 2016 > 21 > 5-6 > 669-681

The human-type ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri (LrPduO) catalyzes the adenosylation of Co(II)rrinoids to generate adenosylcobalamin (AdoCbl) or adenosylcobinamide (AdoCbi⁺). This process requires the formation of “supernucleophilic” Co(I)rrinoid intermediates in the enzyme active site which are properly positioned to abstract the adeonsyl moiety from co-substrate...

article

Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co^Irrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co^IIrrinoids

Kiyoung Park, Paola E. Mera, Theodore C. Moore, Jorge C. Escalante‐Semerena, more

Angewandte Chemie > 127 > 24 > 7264 - 7267

Three distinct families of ATP:corrinoid adenosyltransferases (ACATs) exist that are capable of converting vitamin B₁₂ derivatives into coenzyme B₁₂ by catalyzing the thermodynamically challenging reduction of Co^IIrrinoids to form “supernucleophilic” Co^I intermediates. While the structures and mechanisms of two of the ACAT families have been studied extensively, little is known about the EutT enzymes...

article

Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co^Irrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co^IIrrinoids

Kiyoung Park, Paola E. Mera, Theodore C. Moore, Jorge C. Escalante‐Semerena, more

Angewandte Chemie International Edition > 54 > 24 > 7158 - 7161

Three distinct families of ATP:corrinoid adenosyltransferases (ACATs) exist that are capable of converting vitamin B₁₂ derivatives into coenzyme B₁₂ by catalyzing the thermodynamically challenging reduction of Co^IIrrinoids to form “supernucleophilic” Co^I intermediates. While the structures and mechanisms of two of the ACAT families have been studied extensively, little is known about the EutT enzymes...

article

The structure of S. lividans acetoacetyl‐CoA synthetase shows a novel interaction between the C‐terminal extension and the N‐terminal domain

Carter A. Mitchell, Alex C. Tucker, Jorge C. Escalante‐Semerena, Andrew M. Gulick

Proteins: Structure, Function, and Bioinformatics > 83 > 3 > 575 - 581

The adenosine monoposphate‐forming acyl‐CoA synthetase enzymes catalyze a two‐step reaction that involves the initial formation of an acyl adenylate that reacts in a second partial reaction to form a thioester between the acyl substrate and CoA. These enzymes utilize a Domain Alternation catalytic mechanism, whereby a ∼110 residue C‐terminal domain rotates by 140° to form distinct catalytic conformations...

article

Phylogenetic and amino acid conservation analyses of bacterial l-aspartate-α-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain

Tara N Stuecker, Shanti Bramhacharya, Kelsey M Hodge-Hanson, Garret Suen, more

BMC Research Notes > 2015 > 8 > 1 > 1-11

Background All organisms must synthesize the enzymatic cofactor coenzyme A (CoA) from the precursor pantothenate. Most bacteria can synthesize pantothenate de novo by the condensation of pantoate and β-alanine. The synthesis of β-alanine is catalyzed by l-aspartate-α-decarboxylase (PanD), a pyruvoyl enzyme that is initially synthesized as a zymogen (pro-PanD). Active PanD is generated by self-cleavage...

article

Dissecting cobamide diversity through structural and functional analyses of the base-activating CobT enzyme of Salmonella enterica

Chi Ho Chan, Sean A. Newmister, Keenan Talyor, Kathy R. Claas, more

BBA - General Subjects > 2014 > 1840 > 1 > 464-475

Cobamide diversity arises from the nature of the nucleotide base. Nicotinate mononucleotide (NaMN):base phosphoribosyltransferases (CobT) synthesize α-linked riboside monophosphates from diverse nucleotide base substrates (e.g., benzimidazoles, purines, phenolics) that are incorporated into cobamides.Structural investigations of two members of the CobT family of enzymes in complex with various substrate...

article

Acetoacetyl‐CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans

Alex C. Tucker, Jorge C. Escalante‐Semerena

Molecular Microbiology > 87 > 1 > 152 - 167

GCN5‐type N‐acetyltransferases (GNATs) are enzymes that catalyse the transfer of the acetyl group from acetyl‐CoA to a primary amine. GNATs are conserved in all domains of life. Some members of this family of enzymes acetylate the side‐chain of specific lysine residues in proteins of diverse function. In bacteria, GNAT‐catalysed protein acetylation regulates carbon metabolism, RNA metabolism and transcriptional...

article

A positive selection approach identifies residues important for folding of Salmonella enterica Pat, an Nε-lysine acetyltransferase that regulates central metabolism enzymes

Sandy Thao, Jorge C. Escalante-Semerena

Research in Microbiology > 2012 > 163 > 6-7 > 427-435

In Salmonella enterica, the protein acetyltransferase (Pat) enzyme is part of the sirtuin-dependent acylation/deacylation system (SDPADS) that modulates the activity of several proteins via the acylation of lysine residues critical to their activities. Pat is a ∼98 kDa protein with two distinct domains, an N-terminal acyl-CoA synthetase (NDP-forming) domain (∼700 aa) and a C-terminal acetyltransferase...

article

The missing link in coenzyme A biosynthesis: PanM (formerly YhhK), a yeast GCN5 acetyltransferase homologue triggers aspartate decarboxylase (PanD) maturation in Salmonella enterica

Tara N. Stuecker, Kelsey M. Hodge, Jorge C. Escalante‐Semerena

Molecular Microbiology > 84 > 4 > 608 - 619

Coenzyme A (CoA) is an essential cofactor for all forms of life. The biochemistry underpinning the assembly of CoA in Escherichia coli and other enterobacteria is well understood, except for the events leading to maturation of the L‐aspartate‐α‐decarboxylase (PanD) enzyme that converts pantothenate to β‐alanine. PanD is synthesized as pro‐PanD, which undergoes an auto‐proteolytic cleavage at residue...

article

ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis

Chi Ho Chan, Jorge C. Escalante‐Semerena

Molecular Microbiology > 81 > 4 > 952 - 967

In the homoacetogenic bacterium Sporomusa ovata, phenol and p‐cresol are converted into α‐ribotides, which are incorporated into biologically active cobamides (Cbas) whose lower ligand bases do not form axial co‐ordination bonds with the cobalt ion of the corrin ring. Here we report the identity of two S. ovata genes that encode an enzyme that transfers the phosphoribosyl group of nicotinate mononucleotide...

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Search results for: Jorge C. Escalante-Semerena

In Salmonella enterica, the pathogenicity island 2 (SPI‐2) regulator PagR regulates its own expression and the expression of a five‐gene operon that encodes transketolase C

Localization and interaction studies of the Salmonella enterica ethanolamine ammonia‐lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase

New AMP‐forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation

Staphylococcus aureus modulates the activity of acetyl‐Coenzyme A synthetase (Acs) by sirtuin‐dependent reversible lysine acetylation

Rhodobacterales use a unique L‐threonine kinase for the assembly of the nucleotide loop of coenzyme B₁₂

In Streptomyces lividans, acetyl‐CoA synthetase activity is controlled by O‐serine and N^ɛ‐lysine acetylation

A snapshot of evolution in action: emergence of new heme transport function derived from a coenzyme B₁₂ biosynthetic enzyme

Salmonella enterica synthesizes 5,6‐dimethylbenzimidazolyl‐(DMB)‐α‐riboside. Why some Firmicutes do not require the canonical DMB activation system to synthesize adenosylcobalamin

Conversion of Cobinamide into Coenzyme B₁₂

The EutQ and EutP proteins are novel acetate kinases involved in ethanolamine catabolism: physiological implications for the function of the ethanolamine metabolosome in Salmonella enterica

Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri

Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co^Irrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co^IIrrinoids

Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co^Irrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co^IIrrinoids

The structure of S. lividans acetoacetyl‐CoA synthetase shows a novel interaction between the C‐terminal extension and the N‐terminal domain

Phylogenetic and amino acid conservation analyses of bacterial l-aspartate-α-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain

Dissecting cobamide diversity through structural and functional analyses of the base-activating CobT enzyme of Salmonella enterica

Acetoacetyl‐CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans

A positive selection approach identifies residues important for folding of Salmonella enterica Pat, an Nε-lysine acetyltransferase that regulates central metabolism enzymes

The missing link in coenzyme A biosynthesis: PanM (formerly YhhK), a yeast GCN5 acetyltransferase homologue triggers aspartate decarboxylase (PanD) maturation in Salmonella enterica

ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis

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