Results 31 to 40 of about 6,806 (259)

Compensatory Mutations in Predicted Metal Transporters Modulate Auxin Conjugate Responsiveness in Arabidopsis [PDF]

open access: yes, 2013
Levels of the phytohormone indole-3-acetic acid (IAA) can be altered by the formation and hydrolysis of IAA conjugates. The isolation and characterization of Arabidopsis thaliana mutants with reduced IAA-conjugate sensitivity and wild-type IAA responses ...
Arrivault   +62 more
core   +1 more source

Hormone crosstalk in wound stress response: wound-inducible amidohydrolases can simultaneously regulate jasmonate and auxin homeostasis in Arabidopsis thaliana

open access: yesJournal of Experimental Botany, 2015
Highlight Wound-inducible and ER-located amidohydrolases with overlapping substrate specificities for IAA– and JA–amino acid conjugates regulate the production and destruction of active auxin and JA signals in wounded leaves.
Tong Zhang   +6 more
semanticscholar   +1 more source

Inhibitors of bacterial and plants urease [PDF]

open access: yes, 2013
Urease is an important virulence factor for Helicobacter pylori and Proteus mirabilis as well as in environmental transformations of certain nitrogenous compounds.
Macegoniuk, Katarzyna
core   +1 more source

Combined whole-cell high-throughput functional screening for identification of new nicotinamidases/pyrazinamidases in metagenomic/polygenomic libraries

open access: yesFrontiers in Microbiology, 2016
Nicotinamidases catalyze the hydrolysis of the amide bond in nicotinamide to produce ammonia and nicotinic acid. These enzymes are an essential component of the NAD+ salvage pathway and are implicated in the viability of several pathogenic organisms. Its
Rubén Zapata-Pérez   +4 more
doaj   +1 more source

Systematic site-directed mutagenesis to characterize subunit interactions in E. coli asparaginase II, an enzyme [PDF]

open access: yes, 2005
L-asparaginases (EC 3.5.1.1) catalyze the hydrolysis of L-asparagine to aspartic acid and ammonia. Asparaginases of bacterial origin have been used for over 40 years in the treatment of acute lymphatic leukemia (ALL).
Röhm, Klaus-Heinrich (Prof.)   +1 more
core   +1 more source

Folate Interaction With Genetic Risk for Neural Tube Defects Among Infants in Bangladesh. [PDF]

open access: yesBirth Defects Res
ABSTRACT Background Neural tube defects such as spina bifida (SB) are congenital anomalies associated with significant morbidity and mortality worldwide. Environmental factors, particularly folate, modify SB risk. Based on recurrence rates of SB within families, genetic risk also contributes to SB development.
Mondragon-Estrada E   +13 more
europepmc   +2 more sources

Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides.

open access: yesPLoS ONE, 2015
Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation ...
José P Leite   +6 more
doaj   +1 more source

Tackling Critical Catalytic Residues in Helicobacter pylori L-Asparaginase

open access: yesBiomolecules, 2015
Bacterial asparaginases (amidohydrolases, EC 3.5.1.1) are important enzymes in cancer therapy, especially for Acute Lymphoblastic Leukemia. They are tetrameric enzymes able to catalyze the deamination of L-ASN and, to a variable extent, of L-GLN, on ...
Maristella Maggi   +3 more
doaj   +1 more source

Current Advances in Ochratoxin A-Degrading Enzymes [PDF]

open access: yesShipin Kexue
Ochratoxin A (OTA) poses a serious threat to human and animal health as well as the ecological environment due to its high toxicity, stable physicochemical properties, and widespread occurrence in food and feed.
NIU Zehui, LIANG Zhihong
doaj   +1 more source

Biochemical properties of penicillin amidohydrolase from Micrococcus luteus [PDF]

open access: yesApplied and Environmental Microbiology, 1979
Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36 degrees C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed first-order decay at 36 degrees C.
D H, Nam, D D, Ryu
openaire   +2 more sources

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