Seeing the Process of Histidine Phosphorylation in Human Bisphosphoglycerate Mutase

Wang, Yanli; Liu, Lin; Wei, Zhiyi; Cheng, Zhongjun; Lin, Yangming; Gong, Weimin

doi:10.1074/jbc.m606421200

Cited by 28 publications

(44 citation statements)

References 35 publications

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“…Vanadate readily accepts ligands to form a pentacovalent coordination complex with trigonal bipyramidal geometry (21). The x-ray structures of phosphotransferases complexed with vanadate provide a visual guide to the interactions that occur between active-site residues and the transition state(s) formed along the reaction coordinate that structures of phosphotransferases complexed with phosphate or phosphate ester substrates have, with only a few exceptions (10,(22)(23)(24), failed to do. To demonstrate the existence of a conserved trigonal bipyramidal mold in the HADSF phosphatase subfamily, a phosphate analog is needed that is more resistant to valency expansion than is vandate yet more pliable than orthophosphate (19,25).…”

Section: Resultsmentioning

confidence: 99%

The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state

Dunaway‐Mariano

Allen

2008

Proc. Natl. Acad. Sci. U.S.A.

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The evolution of new catalytic activities and specificities within an enzyme superfamily requires the exploration of sequence space for adaptation to a new substrate with retention of those elements required to stabilize key intermediates/transition states. Here, we propose that core residues in the large enzyme family, the haloalkanoic acid dehalogenase enzyme superfamily (HADSF) form a ''mold'' in which the trigonal bipyramidal transition states formed during phosphoryl transfer are stabilized by electrostatic forces. The vanadate complex of the hexose phosphate phosphatase BT4131 from Bacteroides thetaiotaomicron VPI-5482 (HPP) determined at 1.00 Å resolution via X-ray crystallography assumes a trigonal bipyramidal coordination geometry with the nucleophilic Asp-8 and one oxygen ligand at the apical position. Remarkably, the tungstate in the complex determined to 1.03 Å resolution assumes the same coordination geometry. The contribution of the general acid/base residue Asp-10 in the stabilization of the trigonal bipyramidal species via hydrogen-bond formation with the apical oxygen atom is evidenced by the 1.52 Å structure of the D10A mutant bound to vanadate. This structure shows a collapse of the trigonal bipyramidal geometry with displacement of the water molecule formerly occupying the apical position. Furthermore, the 1.07 Å resolution structure of the D10A mutant complexed with tungstate shows the tungstate to be in a typical ''phosphate-like'' tetrahedral configuration. The analysis of 12 liganded HADSF structures deposited in the protein data bank (PDB) identified stringently conserved elements that stabilize the trigonal bipyramidal transition states by engaging in favorable electrostatic interactions with the axial and equatorial atoms of the transferring phosphoryl group.phosphatase ͉ phosphoryl transfer ͉ transition state stabilization ͉ trigonal bipyramidal phosphorane

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Section: Resultsmentioning

confidence: 99%

The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state

Dunaway‐Mariano

Allen

2008

Proc. Natl. Acad. Sci. U.S.A.

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“…The catalytic reaction of the HP family enzymes is based on the transient phosphorylation of a conserved N-terminal His residue preceded by a conserved Arg (involved in phosphate binding) and followed by a conserved Gly, whose carbonyl oxygen coordinates the side chain of the catalytic His (42,70). These three conserved residues comprise the signature RHG sequence motif of the HP family.…”

Section: Crystal Structure Of Yk23 In a Freementioning

confidence: 99%

Structure and Activity of the Metal-independent Fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae

Kuznetsova

Singer

et al. 2010

Journal of Biological Chemistry

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Fructose-1,6-bisphosphatase (FBPase), a key enzyme of gluconeogenesis and photosynthetic CO 2 fixation, catalyzes the hydrolysis of fructose 1,6-bisphosphate (FBP) to produce fructose 6-phosphate, an important precursor in various biosynthetic pathways. All known FBPases are metal-dependent enzymes, which are classified into five different classes based on their amino acid sequences. Eukaryotes are known to contain only the type-I FBPases, whereas all five types exist in various combinations in prokaryotes. Here we demonstrate that the uncharacterized protein YK23 from Saccharomyces cerevisiae efficiently hydrolyzes FBP in a metal-independent reaction. YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily with homologues found in all organisms. The crystal structure of the YK23 apo-form was solved at Fructose-1,6-bisphosphatase (FBPase) 2 (EC 3.1.3.11) catalyzes the removal of phosphate 1 from fructose 1,6-bisphosphate to produce fructose 6-phosphate, an important precursor in various biosynthetic pathways. FBPase is a key, rate-controlling enzyme of gluconeogenesis, an important metabolic pathway that allows the cells to synthesize glucose and grow on non-carbohydrate carbon sources, such as glycerol, organic acids, and amino acids (1). Gluconeogenesis is also responsible for excessive glucose production found in type 2 diabetes, which is a growing worldwide health concern (2). Because FBPases represent the major control point and function only in gluconeogenesis in mammals, they are recognized as an attractive target for the development of drugs for the treatment of type 2 diabetes (3). FBPase also functions at the branch point between the regenerative phase of the photosynthetic CO 2 fixation cycle (Calvin), which is the primary pathway of carbon fixation, and the starch biosynthesis (4). In addition, FBPase is required for virulence in Mycobacterium tuberculosis and Leishmania major and plays an important role in the production of lysine and glutamate by Corynebacterium glutamicum (5, 6).Most characterized FBPases belong to the superfamily of lithium-sensitive metal-dependent phosphatases that also includes three families of inositol phosphatases (clan CL0171, Pfam data base) (7). Based on the amino acid sequence, FBPases can be assigned to one of the five proposed classes (8 -10). All known FBPases require a divalent metal cation for activity (Mg 2ϩ or Mn 2ϩ ), are inhibited by Li ϩ , and their activity is often regulated by AMP, fructose 2,6-bisphosphate, and phosphoenolpyruvate (11-13). Types I, II, and IV FBPases and inositol monophosphatases have similar three-dimensional structures with a sugar phosphatase-fold (␣␤␣␤␣) suggesting a common evolutionary origin and catalytic mechanism (14 -16). All five types of FBPases are normally found in prokaryotes, where types I, II, and III are more common to bacteria (8), type IV are mostly found in archaea (10), and type V in thermophiles from both domains (9). The majority of organisms have more than one FBPase, mostly the combinatio...

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“…Nayia Petousi, 1 Richard R. Copley, 2,3 Terence R.J. Lappin, 4 Sally E. Haggan, 5 Celeste M. Bento,6 Holger Cario,…”

mentioning

confidence: 99%

Erythrocytosis associated with a novel missense mutation in the BPGM gene

Petousi

Copley²,

Trj.

et al. 2014

Haematologica

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Seeing the Process of Histidine Phosphorylation in Human Bisphosphoglycerate Mutase

Cited by 28 publications

References 35 publications

The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state

The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state

Structure and Activity of the Metal-independent Fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae

Erythrocytosis associated with a novel missense mutation in the BPGM gene

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