BENZOIC ACID,3-AMINO-4-HYDROXY/2-amino-4-carboxyphenol/3-amino-4-hydroxybenzenecarboxylic acid/4-hydroxy-3-amino benzoic acid/3-Amino-4-hydroxy-benzoesaeure/Benzoic acid, 3-amino-4-hydroxy-/3-AMINO-4-HYDROXYBENZOIC ACID USP/3-amino-4-hydroxy-benzoic acid/3-amino-4-hydroxybnzoic acid/3-Amino-4-hydroxybenzoic acid/3-AMino-4-hydroxybenzoic acid 5GR
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Among quadrupedal gaits, the galloping gait has specific characteristics in terms of locomotor behavior. In particular, it shows a left-right asymmetry in gait parameters such as touchdown angle and the relative phase of limb movements. In addition, asymmetric gait parameters show a characteristic dependence on locomotion speed. There are two types of galloping gaits in quadruped animals: the transverse gallop, often observed in horses; and the rotary gallop, often observed in dogs and cheetahs. These two gaits have different footfall sequences. Although these specific characteristics in quadrupedal galloping gaits have been observed and described in detail, the underlying mechanisms remain unclear. In this paper, we use a simple physical model with a rigid body and four massless springs and incorporate the left-right asymmetry of touchdown angles. Our simulation results show that our model produces stable galloping gaits for certain combinations of model parameters and explains these specific characteristics observed in the quadrupedal galloping gait. The results are then evaluated in comparison with the measured data of quadruped animals and the gait mechanisms are clarified from the viewpoint of dynamics, such as the roles of the left-right touchdown angle difference in the generation of galloping gaits and energy transfer during one gait cycle to produce two different galloping gaits.
Center of mass movement; Energy transfer; Galloping gait; Left-right asymmetry; Model; Quadruped; Touchdown angle.
A Galloping Quadruped Model Using Left-Right Asymmetry in Touchdown Angles
Masayasu Tanase 1, Yuichi Ambe 1, Shinya Aoi 2, Fumitoshi Matsuno 1
2015 Sep 18
The production of the bioplastic precursor 3-amino-4-hydroxybenzoic acid (3,4-AHBA) from sweet sorghum juice, which contains amino acids and the fermentable sugars sucrose, glucose and fructose, was assessed to address the limitations of producing bio-based chemicals from renewable feedstocks. Recombinant Corynebacterium glutamicum strain KT01 expressing griH and griI derived from Streptomyces griseus produced 3,4-AHBA from the sweet sorghum juice of cultivar SIL-05 at a final concentration (1.0 g l(-1)) that was 5-fold higher than that from pure sucrose. Fractionation of sweet sorghum juice by nanofiltration (NF) membrane separation (molecular weight cut-off 150) revealed that the NF-concentrated fraction, which contained the highest concentrations of amino acids, increased 3,4-AHBA production, whereas the NF-filtrated fraction inhibited 3,4-AHBA biosynthesis. Amino acid supplementation experiments revealed that leucine specifically enhanced 3,4-AHBA production by strain KT01. Taken together, these results suggest that sweet sorghum juice is a potentially suitable feedstock for 3,4-AHBA production by recombinant C. glutamicum.
3-Amino-4-hydroxybenzoic acid; Biomass; Corynebacterium glutamicum; Membrane separation; Sweet sorghum juice.
3-Amino-4-hydroxybenzoic Acid Production From Sweet Sorghum Juice by Recombinant Corynebacterium Glutamicum
Hideo Kawaguchi 1, Kengo Sasaki 2, Kouji Uematsu 1, Yota Tsuge 2, Hiroshi Teramura 1, Naoko Okai 2, Sachiko Nakamura-Tsuruta 1, Yohei Katsuyama 3, Yoshinori Sugai 3, Yasuo Ohnishi 3, Ko Hirano 4, Takashi Sazuka 4, Chiaki Ogino 1, Akihiko Kondo 5
Human COQ6 encodes a monooxygenase which is responsible for the C5-hydroxylation of the quinone ring of coenzyme Q (CoQ). Mutations in COQ6 cause primary CoQ deficiency, a condition responsive to oral CoQ10 supplementation. Treatment is however still problematic given the poor bioavailability of CoQ10. We employed S. cerevisiae lacking the orthologous gene to characterize the two different human COQ6 isoforms and the mutations found in patients. COQ6 isoform a can partially complement the defective yeast, while isoform b, which lacks part of the FAD-binding domain, is inactive but partially stable, and could have a regulatory/inhibitory function in CoQ10 biosynthesis. Most mutations identified in patients, including the frameshift Q461fs478X mutation, retain residual enzymatic activity, and all patients carry at least one hypomorphic allele, confirming that the complete block of CoQ biosynthesis is lethal. These mutants are also partially stable and allow the assembly of the CoQ biosynthetic complex. In fact treatment with two hydroxylated analogues of 4-hydroxybenzoic acid, namely, vanillic acid or 3-4-hydroxybenzoic acid, restored the respiratory growth of yeast Δcoq6 cells expressing the mutant huCOQ6-isoa proteins. These compounds, and particularly vanillic acid, could therefore represent an interesting therapeutic option for COQ6 patients.
3,4 diHB; 3,4 dihydroxybenzoic acid; 4-hydroxybenzoate; 4HB; COQ6; COQ8-ADCK3; CYC1; CoQ; CoQ(10); Coenzyme Q; FAD; SRNS; Steroid-resistant nephrotic syndrome; VA; Vanillic acid; aarF domain containing kinase 3; coenzyme Q; coenzyme Q(10); cytochrome c1; flavin adenine dinucleotide; flavin-dependent monooxygenase; pHBH; para-hydroxybenzoate hydroxylase; steroid resistant nephrotic syndrome; vanillic acid.
Effect of Vanillic Acid on COQ6 Mutants Identified in Patients With Coenzyme Q10 Deficiency
Mara Doimo 1, Eva Trevisson, Rannar Airik, Marc Bergdoll, Carlos Santos-OcaNa, Friedhelm Hildebrandt, Placido Navas, Fabien Pierrel, Leonardo Salviati