Results 141 to 150 of about 79,493 (196)

Direct asymmetric synthesis of β-branched aromatic α-amino acids using engineered phenylalanine ammonia lyases. [PDF]

open access: yesNat Commun
Sun C   +12 more
europepmc   +1 more source

Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP. [PDF]

open access: yesNat Commun
Bicer D   +13 more
europepmc   +1 more source

Demethylation of methylguanidine by a stepwise dioxygenase and lyase reaction. [PDF]

open access: yesNat Commun
Sinn M   +5 more
europepmc   +1 more source

Diversity-oriented photobiocatalytic synthesis via stereoselective three-component radical coupling. [PDF]

open access: yesScience
Zhang C   +8 more
europepmc   +1 more source

Properties and distribution of mammalian l-cysteine sulfinate carboxy-lyases

open access: yesBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
Abstract 1. 1. [1-14C]Cysteine sulfinic acid (CySO2H) and [1-14C]cysteic acid (CySO3H) were synthesized and some characteristics of the decarboxylation of these amino acids studied in partially purified rat-liver and brain preparations. 2. 2. The apparent Km's for CySO2H and CySO3H were found to be about 10 times lower in liver than in brain.
J G, JACOBSEN, L L, THOMAS, L H, SMITH
semanticscholar   +4 more sources

Comparison of L-aspartate 4-carboxy-lyases ofCunninghamella elegansandPenicillium citrinum

open access: yesMicrobiological Research, 1994
L-Aspartate 4-carboxy-lyase of Cunninghamella elegans and Penicillium citrinum has a pH optimum of 5.5. Maximal activity of both enzymes is obtained at 40 degrees C, and both are thermolabile. The Km of the C. elegans enzyme for L-aspartate is 25 mM, while that of the P. citrinum enzyme is 27 mM. The two enzymes are specific for L-aspartate.
T. A. El-Rahmany
semanticscholar   +5 more sources

Biologically generated carbon dioxide: nature's versatile chemical strategies for carboxy lyases

Natural Product Reports, 2020
Metabolic production of CO2is natural product chemistry on a mammoth scale.
C. Walsh
openaire   +3 more sources

Deciphering the properties and reaction mechanism of anhydromevalonate phosphate decarboxylase, a prenylated flavin mononucleotide-dependent enzyme in the archaeal mevalonate pathway.

open access: yesThe FEBS Journal, EarlyView.
In the archaeal mevalonate pathway, the prototype of all existing mevalonate pathways, a unique intermediate, trans-anhydromevalonate phosphate, is decarboxylated to form isopentenyl phosphate.
Rino Ishikawa   +9 more
semanticscholar   +2 more sources

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