Effects of various compounds on histidine decarboxylase activity: Active site mapping

Sakamoto, Y; Watanabe, Tetsu; Hayashi, Hideyuki; Taguchi, Yoshitaka; Wada, Hiroshi

doi:10.1007/bf01966677

Cited by 12 publications

(4 citation statements)

References 14 publications

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“…This binding mode of the coenzymesubstrate conjugate in the active site of hHDC demonstrates that the imidazole binding moiety of substrate consists of a tightly packed and specific pocket in contrast to that of pDDC ( Fig. 5A-C) (38). Tyr-81B in hHDC adopted a "closed conformation" in contrast to the "open conformation" of the corresponding residue Phe-80B in pDDC and can form a stacking interaction with the imidazole ring and an additional hydrogen bond with the N1 atom of the imidazole ring (Fig.…”

Section: Discussionmentioning

confidence: 96%

Inhibitory and structural studies of novel coenzyme‐substrate analogs of human histidine decarboxylase

Wu¹,

Gehring³

2007

FASEB j.

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Histamine, a biogenic amine with important biological functions, is produced from histidine by histidine decarboxylase (HDC), a pyridoxal 5'-phosphate-dependent enzyme. HDC is thus a potential target to attenuate histamine production in certain pathological states. Targeting mammalian HDC with novel inhibitors and elucidating the structural basis of their specificity for HDC are challenging tasks, because the three-dimensional structure of mammalian HDC is still unknown. In the present study, we designed, synthesized, and tested potentially membrane-permeable pyridoxyl-substrate conjugates as inhibitors for human (h) HDC and modeled an active site of hHDC, which is compatible with the experimental data. The most potent inhibitory compound among nine tested structural variants was the pyridoxyl-histidine methyl ester conjugate (PHME), indicating that the binding site of hHDC does not tolerate groups other than the imidazole side chain of histidine. PHME inhibited 60% of the fraction of 12-O-tetradecanoylphorbol-13-acetate-induced newly synthesized HDC in human HMC-1 cells at 200 microM and was also inhibitory in cell extracts. The proposed model of hHDC, containing phosphopyridoxyl-histidine in the active site, revealed the binding specificity of HDC toward its substrate and the structure-activity relationship of the designed and investigated compounds.

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Section: Discussionmentioning

confidence: 96%

Inhibitory and structural studies of novel coenzyme‐substrate analogs of human histidine decarboxylase

Wu¹,

Gehring³

2007

FASEB j.

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“…In addition, the pro-histaminic pathway is tissue-dependent. Indeed, carnosine is an inhibitor of histidine decarboxylase [131], and it has been shown that histamine release from mast cell is decreased after carnosine treatment [132]. Therefore, antioxidant and carbonyl-scavenging activity, as well as pro-histaminic properties may contribute to the effect of carnosine in different tissues under a variety of physiological and pathological conditions.…”

Section: Mechanisms Of In Vivo Action Of Carnosine: Pre-clinical Amentioning

confidence: 99%

Detoxification of aldehydes by histidine-containing dipeptides: From chemistry to clinical implications

Xie

Baba

Sweeney

et al. 2013

Chemico-Biological Interactions

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Aldehydes are generated by oxidized lipids and carbohydrates at increased levels under conditions of metabolic imbalance and oxidative stress during atherosclerosis, myocardial and cerebral ischemia, diabetes, neurodegenerative diseases and trauma. In most tissues, aldehydes are detoxified by oxidoreductases that catalyze the oxidation or the reduction of aldehydes or enzymatic and nonenzymatic conjugation with low molecular weight thiols and amines, such as glutathione and histidine dipeptides. Histidine dipeptides are present in micromolar to millimolar range in the tissues of vertebrates, where they are involved in a variety of physiological functions such as pH buffering, metal chelation, oxidant and aldehyde scavenging. Histidine dipeptides such as carnosine form Michael adducts with lipid-derived unsaturated aldehydes, and react with carbohydrate-derived oxo- and hydroxy- aldehydes forming products of unknown structure. Although these peptides react with electrophilic molecules at lower rate than glutathione, they can protect glutathione from modification by oxidant and they may be important for aldehyde quenching in glutathione-depleted cells or extracellular space where glutathione is scarce. Consistent with in vitro findings, treatment with carnosine has been shown to diminish ischemic injury, improve glucose control, ameliorate the development of complications in animal models of diabetes and obesity, promote wound healing and decrease atherosclerosis. The protective effects of carnosine have been linked to its anti-oxidant properties, it ability to promote glycolysis, detoxify reactive aldehydes and enhance histamine levels. Thus, treatment with carnosine and related histidine dipeptides may be a promising strategy for the prevention and treatment of diseases associated with high carbonyl load.

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“…Such a process occurs, for example, with preserved fish, and urocanic acid has been proposed as a spoilage index [13]. It is also known that urocanic acid is an inhibitor of histidine decarboxylase [14] and that it has specific toxicity towards certain neoplastic cells [15]. Moreover, being subjected to a ( E / Z ) photoisomerization [ 161, urocanic acid may find use to protect the human epidermis from solar radiations [ 171.…”

Section: A R = H B R = a Cmentioning

confidence: 99%

ChemInform Abstract: Sarcodictyin A (Ia) and Sarcodictyin B (Ib), Novel Diterpenoidic Alcohols Esterified by (E)‐N(1)‐Methylurocanic Acid. Isolation from the Mediterranean Stolonifer Sarcodictyon roseum.

D’Ambrosio¹,

Guerriero²,

Pietra³

1988

ChemInform

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Effects of various compounds on histidine decarboxylase activity: Active site mapping

Cited by 12 publications

References 14 publications

Inhibitory and structural studies of novel coenzyme‐substrate analogs of human histidine decarboxylase

Inhibitory and structural studies of novel coenzyme‐substrate analogs of human histidine decarboxylase

Detoxification of aldehydes by histidine-containing dipeptides: From chemistry to clinical implications

ChemInform Abstract: Sarcodictyin A (Ia) and Sarcodictyin B (Ib), Novel Diterpenoidic Alcohols Esterified by (E)‐N(1)‐Methylurocanic Acid. Isolation from the Mediterranean Stolonifer Sarcodictyon roseum.

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