Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Erythrocyte and serum enzyme system in the Gagu of the Ivory Coast have been investigated. Some systems (e.g. PGM) differ little between the subdivisions of the Gagu group, but others differ considerably (e.g. G6PD variants). In general the red cell enzyme frequencies fall within the range of variation characteristic of African populations. Serum cholinesterase variants are present only at low frequency, and the distribution of alkaline phosphatase phenotype shows the expected correlation with ABO blood groups.
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PMID:Polymorphism of erythrocyte and serum enzyme systems in the Gagu of the Ivory Coast. 18 37

Blood samples from 109 Siriono (Eastern Bolivia) belonging to the Tupi-Guarani group were investigated for enzyme variants in the following systems: glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, adenylate kinase, phospho-glucomutase (locus 1 and 2), acid phosphatases, lactate dehydrogenase, NADH diaphorase, pseudocholinesterase (E1 and E2 locus), and serum alkaline phosphatase. The most relevant observations are: (1) A relative lack of polymorphism, a characteristic feature of the Amerindian populations studied up to now. These data are consistent with the hypothesis of a 'common ancestral background' in Indian populations whatever the degree of sociocultural and linguistic diversity, and the geographical distances. (2) Specific traits due to the frequency of alleles in some systems confer to that tribe a particular position among Amerindians. The effects of genetic drift may be postulated in order to explain the high rate of PGM and 6PGD polymorphism. Furthermore, in that small community, the disappearance of some alleles (pa gene) can plausibly be explained in terms of a balanced influence of mutational and selective pressure.
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PMID:Serum and red cell enzyme variants in an Amerindian tribe: the Sirionos (Eastern Bolivia). 97 93

The primary sequence of maize 2,3-bisphosphoglycerate-independent phosphoglycerate mutase was deduced from cDNAs isolated from maize cDNA libraries by screening with specific antibodies to the cofactor-independent enzyme and from a maize genomic clone. The genomic clone provided the 5'-nucleotide sequence encoding the N-terminal amino acids which could not be obtained from the cDNA. Confirmation that the nucleotide sequence was for the cofactor-independent phosphoglycerate mutase was obtained by sequencing the peptides generated from cyanogen bromide cleavage of the purified protein. This is the first report of the amino acid sequence of a 2,3-bisphosphoglycerate cofactor-independent phosphoglycerate mutase, which consists of 559 amino acids and is twice the molecular size of the mammalian cofactor-dependent enzyme subunit. Analysis of the cofactor-independent phosphoglycerate mutase amino acid sequence revealed no identity with the cofactor-dependent mutase types. Northern blot analysis confirmed this difference since the maize cofactor-independent phosphoglycerate mutase cDNA did not hybridize with mRNA of the cofactor-dependent mutase. The lack of amino acid identity between cofactor-dependent and -independent enzymes is consistent with their different catalytic mechanisms and suggests that both enzymes are unrelated evolutionarily and arose from two independent ancestral genes. However, a constellation of residues which are involved in metal ion binding in various alkaline phosphatases is conserved in the maize cofactor-independent phosphoglycerate mutase, which suggests that the enzyme is a member of the alkaline phosphatase family of enzymes.
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PMID:Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize. Possible relationship to the alkaline phosphatase family. 153 26

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

The screening of autopsy specimens, vaginal, buccal, and rectal swabs, for the presence of seminal fluid in rape homicide investigations utilizing classical techniques can lead to erroneous results. In the absence of spermatozoa, techniques are needed which can help to identify seminal fluid. This report illustrates the use of a multi-enzyme electrophoretic approach identifying seminal acid phosphatase (SAP) and lactic acid dehydrogenase (LDH-X) as an initial screening procedure. Subsequent analyses for the presence of acid and alkaline phosphatase (semiquantitative) yield information which can help identify false-positive SAP's. Additionally, salivary amylase can be tentatively identified using the same multi-enzyme procedure which informs the investigator of possible salivary contamination of the sample and possible erroneous PGM results. Statistics utilizing the multi-enzyme approach in case work are also presented.
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PMID:A multi-enzyme electrophoretic system for the identification of seminal fluid from postmortem specimens. 617 21

Sequence analysis of the probable archaeal phosphoglycerate mutase resulted in the identification of a superfamily of metalloenzymes with similar metal-binding sites and predicted conserved structural fold. This superfamily unites alkaline phosphatase, N-acetylgalactosamine-4-sulfatase, and cerebroside sulfatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulfatases. In addition to the metal-binding motifs, all these enzymes contain a set of conserved amino acid residues that are likely to be required for the enzymatic activity. Mutational changes in the vicinity of these residues in several sulfatases cause mucopolysaccharidosis (Hunter, Maroteaux-Lamy, Morquio, and Sanfilippo syndromes) and metachromatic leucodystrophy.
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PMID:A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. 1008 81

Assays of phosphoglycerate mutase (PGAM) activity in lysates of bloodstream form Trypanosoma brucei appeared not to require exogenous 2,3-bisphosphoglycerate, thus suggesting that this protist contains an enzyme belonging to the class of cofactor-independent PGAMs. A gene encoding a polypeptide with motifs characteristic for this class of enzymes was cloned. The predicted T. brucei PGAM polypeptide contains 549 amino acids, with Mr 60 557 and pI 5.5. Comparison with 15 cofactor-independent PGAM sequences available in databases showed that the amino-acid sequence of the trypanosome enzyme has 59-62% identity with plant PGAMs and 29-35% with eubacterial enzymes. A low 28% identity was observed with the only available invertebrate sequence. The trypanosome enzyme has been expressed in Escherichia coli, purified to homogeneity and subjected to preliminary kinetic analysis. Previous studies have shown that cofactor-dependent and -independent PGAMs are not homologous. It has been inferred that the cofactor-independent PGAMs are in fact homologous to a family of metalloenzymes containing alkaline phosphatases and sulphatases. Prediction of the secondary structure of T. brucei PGAM and threading the sequence into the known crystal structure of E. coli alkaline phosphatase (AP) confirmed this homology, despite the very low sequence identity. Generally, a good match between predicted (PGAM) and actual (AP) secondary structure elements was observed. In contrast to trypanosomes, glycolysis in all vertebrates involves a cofactor-dependent PGAM. The presence of distinct nonhomologous PGAMs in the parasite and its human host offers great potential for the design of selective inhibitors which could form leads for new trypanocidal drugs.
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PMID:Trypanosoma brucei contains a 2,3-bisphosphoglycerate independent phosphoglycerate mutase. 1069 85

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-A 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.
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PMID:Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. 1076 95

Recombinant cofactor-independent phosphoglycerate mutase from Trypanosoma brucei was inactivated by EDTA, and reactivated by Co(2+) much more than by Mn(2+) or Fe(2+). It displayed a minor phosphoglycerate phosphatase activity, which was stimulated by Mn(2+) more than by Co(2+). Upon incubation with [(32)P]phosphoglycerate, radioactivity was incorporated into the enzyme, most particularly in the presence of Mn(2+) or Fe(2+). The phosphorylated residue was identified by tandem mass spectrometry as Ser74, a residue homologous to the phosphorylated serine in alkaline phosphatase. However, the rates of formation and of disappearance of this phosphoenzyme were quite low compared to the mutase reaction. This and other properties indicated that the observed phosphoenzyme is an intermediate in the minor phosphatase activity rather than in the phosphomutase reaction.
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PMID:The 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from Trypanosoma brucei: metal-ion dependency and phosphoenzyme formation. 1168 75

Cofactor-independent phosphoglycerate mutase (iPGM) has been previously identified as a member of the alkaline phosphatase (AlkP) superfamily of enzymes, based on the conservation of the predicted metal-binding residues. Structural alignment of iPGM with AlkP and cerebroside sulfatase confirmed that all these enzymes have a common core structure and revealed similarly located conserved Ser (in iPGM and AlkP) or Cys (in sulfatases) residues in their active sites. In AlkP, this Ser residue is phosphorylated during catalysis, whereas in sulfatases the active site Cys residues are modified to formylglycine and sulfatated. Similarly located Thr residue forms a phosphoenzyme intermediate in one more enzyme of the AlkP superfamily, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1 (autotaxin). Using structure-based sequence alignment, we identified homologous Ser, Thr, or Cys residues in other enzymes of the AlkP superfamily, such as phosphopentomutase, phosphoglycerol transferase, phosphonoacetate hydrolase, and GPI-anchoring enzymes (glycosylphosphatidylinositol phosphoethanolamine transferases) MCD4, GPI7, and GPI13. We predict that catalytical cycles of all the enzymes of AlkP superfamily include phosphoenzyme (or sulfoenzyme) intermediates.
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PMID:Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes. 1174 79


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