Phylogeny and ontogeny of the phosphoglycerate mutases—IV. Distribution of glycerate-2,3-P2 dependent and independent phosphoglycerate mutases in algae, fungi, plants and animals

Carreras, José; Mezquita, Jovita; Bosch, Joan; Bartrons, Ramón; Pons, Gabriel

doi:10.1016/0305-0491(82)90467-9

Cited by 22 publications

(30 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…wheat germ), filamentous fungi (e.g. Aspergillus nidulans), Bacillus sp., coelenterates and arachnids are active in the absence of this cofactor (Grisolia & Joyce, 1959; Ray & Peck, 1972;Carreras et al, 1982;. In contrast with the cofactor-dependent enzymes, for which much structural anl mechanistic knowledge is available (see, e.g., Winn et al, 1981), very little is known about the cofactorindependent enzymcs.…”

Section: Introductionmentioning

confidence: 99%

Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

Johnson

Price

1988

Biochemical Journal

View full text Add to dashboard Cite

It has been reported [Smith, McWilliams & Hass (1986) Biochem. Biophys. Res. Commun. 136, 336-340] that addition of certain metal ions, notably Co2+ and Mn2+, promoted the refolding of denatured phosphoglycerate mutase from wheat germ. We have re-investigated these experiments and have shown that, when precautions are taken to avoid artefacts in the assay system, the metal ions do not promote any re-activation of the denatured wheat-germ or Aspergillus nidulans enzymes. An alternative explanation is offered for the observations of Smith et al. (1986).

show abstract

Section: Introductionmentioning

confidence: 99%

Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

Johnson

Price

1988

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…In contrast, dPGM is composed of ϳ250 amino acids and catalyzes the intermolecular transfer of the phospho group between the monophosphoglycerates and the cofactor (2,3-diphosphoglycerate) through a phosphohistidine intermediate (10). Vertebrates are known to possess the dPGM form exclusively, whereas in other organisms, the distribution of the two forms has been considered complex and unpredictable because either dPGM or iPGM or both forms may be present (11,12). Whereas the two forms of PGM are distinct, the amino acid sequence of each form when present is conserved from bacteria to higher eukaryotes (13).…”

mentioning

confidence: 99%

Cofactor-independent Phosphoglycerate Mutase Has an Essential Role in Caenorhabditis elegans and Is Conserved in Parasitic Nematodes

Zhang

Foster

Kumar

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Phosphoglycerate mutases catalyze the interconversion of 2-and 3-phosphoglycerate in the glycolytic and gluconeogenic pathways. They exist in two unrelated forms that are either cofactor (2,3-diphosphoglycerate)-dependent or cofactor-independent. The two enzymes have no similarity in amino acid sequence, tertiary structure, or catalytic mechanism. Certain organisms including vertebrates have only the cofactor-dependent form, whereas other organisms can possess the independent form or both. Caenorhabditis elegans has been predicted to have only independent phosphoglycerate mutase. In this study, we have cloned and produced recombinant, independent phosphoglycerate mutases from C. elegans and the human-parasitic nematode Brugia malayi. They are 70% identical to each other and related to known bacterial, fungal, and protozoan enzymes. The nematode enzymes possess the catalytic serine, and other key amino acids proposed for catalysis and recombinant enzymes showed typical phosphoglycerate mutase activities in both the glycolytic and gluconeogenic directions. The gene is essential in C. elegans, because the reduction of its activity by RNA interference led to embryonic lethality, larval lethality, and abnormal body morphology. Promoter reporter analysis indicated widespread expression in larval and adult C. elegans with the highest levels apparent in the nerve ring, intestine, and body wall muscles. The enzyme was found in a diverse group of nematodes representing the major clades, indicating that it is conserved throughout this phylum. Our results demonstrate that nematodes, unlike vertebrates, utilize independent phosphoglycerate mutase in glycolytic and gluconeogenic pathways and that the enzyme is probably essential for all nematodes.

show abstract

“…The reasons for enzyme inactivity are not clear, but probably include the crystallization temperature (B. stearothermophilus iPGM has maximum activity at 65°C), the low pH (4), and the presence of a variety of salts including Zn 2ϩ ions, which inhibit iPGM. 3 However, the presence of Mn 2ϩ but not Zn 2ϩ ions in the iPGM active site was clearly established based on the crystallographic analyses and refinements. The square pyramidal coordination geometry of the active site metal ions is also indicative of the presence of Mn 2ϩ , since Zn 2ϩ would have tetrahedral geometry (17).…”

mentioning

confidence: 99%

“…They also have the ability to perform all reactions noted above but at significantly different rates. The monophosphoglycerate mutases that do not require DPG for catalysis are termed 23PGA-independent (iPGMs) and are the predominant PGM in plants and some other bacteria, including endosporeforming Gram-positive bacteria and their close relatives; iPGMs, unlike cofactor-dependent phosphoglycerate mutases and bisphosphoglycerate mutases, can only carry out the interconversion of 2PGA and 3PGA (1,3,4). The two classes of monophosphoglycerate mutases are extremely different in amino acid sequence, catalytic mechanism, and structure, both tertiary and quaternary.…”

mentioning

confidence: 99%

Mechanism of Catalysis of the Cofactor-independent Phosphoglycerate Mutase from Bacillus stearothermophilus

Jedrzejas¹,

Chander²,

Setlow³

et al. 2000

Journal of Biological Chemistry

100

View full text Add to dashboard Cite

The structure of the complex between the 2,3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain further evidence for this mechanism, we have solved the structure of this iPGM complexed with 2-phosphoglycerate and two Mn 2؉ ions at 1.7-Å resolution. The structure consists of two different domains connected by two loops and interacting through a network of hydrogen bonds. This structure is consistent with the proposed mechanism for iPGM catalysis, with the two main steps in catalysis being a phosphatase reaction removing the phosphate from 2-or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The structure also allowed the assignment of the function of the two domains of the enzyme, one of which participates in the phosphatase reaction and formation of the phosphoserine enzyme intermediate, with the other involved in the phosphotransferase reaction regenerating phosphoglycerate. Significant structural similarity has also been found between the active site of the iPGM domain catalyzing the phosphatase reaction and Escherichia coli alkaline phosphatase. Phosphoglycerate mutases (PGMs)1 catalyze three types of reactions including interconversion of 1,3-phosphoglycerate and 2,3-phosphoglycerate (23PGA) and of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA) as well as synthesis of 3PGA from 23PGA (1). There are two distinct types of PGMs, bisphosphoglycerate mutase and monophosphoglycerate mutase, and only the first type has the ability to perform all of the reactions listed above, while monophosphoglycerate mutases catalyze primarily the interconversion of 3PGA and 2PGA in both glycolysis and gluconeogenesis. There are also two classes of monophosphoglycerate mutases that are distinguished by their requirement for 23PGA for catalysis (1, 2). The PGMs requiring 23PGA for catalysis are termed 23PGA-dependent and are the predominant PGM in mammals, yeast, and some bacteria. They also have the ability to perform all reactions noted above but at significantly different rates. The monophosphoglycerate mutases that do not require DPG for catalysis are termed 23PGA-independent (iPGMs) and are the predominant PGM in plants and some other bacteria, including endosporeforming Gram-positive bacteria and their close relatives; iPGMs, unlike cofactor-dependent phosphoglycerate mutases and bisphosphoglycerate mutases, can only carry out the interconversion of 2PGA and 3PGA (1, 3, 4). The two classes of monophosphoglycerate mutases are extremely different in amino acid sequence, catalytic mechanism, and structure, both tertiary and quaternary. Despite the differences between these two types of PGMs, the iPGMs all have very conserved amino acid sequences, as do the cofactor-d...

show abstract

Phylogeny and ontogeny of the phosphoglycerate mutases—IV. Distribution of glycerate-2,3-P2 dependent and independent phosphoglycerate mutases in algae, fungi, plants and animals

Cited by 22 publications

References 26 publications

Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

Cofactor-independent Phosphoglycerate Mutase Has an Essential Role in Caenorhabditis elegans and Is Conserved in Parasitic Nematodes

Mechanism of Catalysis of the Cofactor-independent Phosphoglycerate Mutase from Bacillus stearothermophilus

Contact Info

Product

Resources

About