Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by <scp>l</scp>-leucine

Hümmer, Christine; Millán, José Luis

doi:10.1042/bj2740091

Cited by 44 publications

(40 citation statements)

References 24 publications

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“…Also, activation of ALP activity is facilitated by divalent cations such as magnesium (Mg 2+ ) (Kim and Wyckoff, 1990;Le Du et al, 2001;Dean, 2002) and colbalt (Co 2+ ) (Arise et al, 2008). Conversely, ALPs are inactivated/inhibited by wide range of compounds, depending on the source or/and isoenzymic form of the enzyme (Hummer and Milla´n, 1991;Hoylaerts et al, 1992). For instance, bone and kidney ALPs are inhibited by urea, whereas those obtained from *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Kinetic studies of alkaline phosphatase extracted from rabbit (Lepus townsendii) liver

Njoku¹,

Chikezie²,

Kaoje³

2011

Afr. J. Biotechnol.

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Section: Introductionmentioning

confidence: 99%

Kinetic studies of alkaline phosphatase extracted from rabbit (Lepus townsendii) liver

Njoku¹,

Chikezie²,

Kaoje³

2011

Afr. J. Biotechnol.

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“…L-homoarginine strongly inhibits tissue-nonspecific ALP and levamisole inhibits placental and tissue-nonspecific isoenzymes. Levamisole, L-phenylalanine and Lhomoarginine, which permit discrimination between tissue-nonspecific and tissue-specific ALPs, have been used for the clinical quantitation and identification of ALP isoenzymes for almost a century (2,24,25,30). Vanadate is an ALP inhibitor (12,17,31).…”

Section: Results Results Results Resultsmentioning

confidence: 99%

“…Unlike mammalian ALPs, bacterial ALPs are not stereospecifically inhibited by L-amino acids through a non-competitive mechanism (1)(2)(3)17,(23)(24)(25).…”

Section: Introduction Introduction Introduction Introduction Introducmentioning

confidence: 99%

In vitro modulation of alkaline phosphatase activity of Saccharomyces cerevisiae grown in low or high phosphate medium

Fernandes

Amorim

Azevedo

et al. 2007

Braz J Med Biol Res

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Our objective was to characterize the modulation of the activity of Saccharomyces cerevisiae alkaline phosphatases (ALPs) by classic inhibitors of ALP activity, cholesterol and steroid hormones, in order to identify catalytic similarities between yeast and mammalian ALPs. S. cerevisiae expresses two ALPs, coded for by the PHO8 and PHO13 genes. The product of the PHO8 gene is repressible by Pi in the medium. ALP activity from yeast (grown in low or high phosphate medium) homogenates was determined with p-nitrophenylphosphate as substrate, pH 10.4 (lPiALP or hPiALP, respectively). Activation of hPiALP was observed with 5 mM L-amino acids (L-homoarginine -186%, L-leucine -155% and L-phenylalanine -168%) and with 1 mM levamisole (122%; percentage values, in comparison to control, of recovered activity). EDTA (5 mM) and vanadate (1 mM) distinctly inhibited hPiALP (2 and 20%, respectively). L-homoarginine (5 mM) had a lower activating effect on lPiALP (166%) and was the strongest hPiALP activator. Corticosterone (5 mM) inhibited hPiALP to 90%, but no effect was observed in low phosphate medium. Cholesterol, ß-estradiol and progesterone also had different effects on lPiALP and hPiALP. A concentrationdependent activation of lPiALP minus hPiALP was evident with all three compounds, most especially with ß-estradiol and cholesterol. These results do not allow us to identify similarities of the behavior of S. cerevisiae ALPs and any of the mammalian ALPs but allow us to raise the hypothesis of differential regulation of S. cerevisiae ALPs by L-homoarginine, ß-estradiol and cholesterol and of using these compounds to discriminate between S. cerevisiae lPiALP and hPiALP.

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“…Furthermore, H434, which corresponds to E429 in PLAP, is substituted by a glutamine residue in the chicken sequence. This position is involved in the uncompetitive inhibition mechanism of PLAP and human GCAP (Hoylaerts et al, 1992;Hummer and Millan, 1991) but it is unclear how this substitution determines the uncompetitive inhibition properties of TNAP by levamisole and L-homoarginine.…”

Section: Discussionmentioning

confidence: 99%

Tissue‐nonspecific alkaline phosphatase participates in the establishment and growth of feather germs in embryonic chick skin cultures

Crawford

Weissig

Binette

et al. 1995

Developmental Dynamics

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Alkaline phosphatase activity is present in the mesoderm of embryonic chick skin and becomes spatially restricted to the dermal condensation of the developing feather germs. Inhibitors to tissue-nonspecific (liver/bone/kidney), but not intestinal, alkaline phosphatase inhibit the establishment and growth of feather germs in cultured skins. A window of maximum sensitivity to the inhibitor was observed to be the first day of culture when early development and establishment of pattern takes place. The cDNA for the avian tissue-nonspecific alkaline phosphatase was cloned and sequenced, and Southern analysis revealed a single copy of this gene in the avian genome. Northern analysis revealed that a 2.8 kb transcript for this form of alkaline phosphatase is present in developing skin. o 1995 Wiley-Liss, Inc.

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Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by l-leucine

Cited by 44 publications

References 24 publications

Kinetic studies of alkaline phosphatase extracted from rabbit (Lepus townsendii) liver

Kinetic studies of alkaline phosphatase extracted from rabbit (Lepus townsendii) liver

In vitro modulation of alkaline phosphatase activity of Saccharomyces cerevisiae grown in low or high phosphate medium

Tissue‐nonspecific alkaline phosphatase participates in the establishment and growth of feather germs in embryonic chick skin cultures

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