A novel method of producing high-purity hydroxy-L-pipecolic acids in an efficient and inexpensive manner while suppressing the production of hydroxy-L-proline is provided. The method includes allowing an L-pipecolic acid hydroxylase, a microorganism or cell having the ability to produce the enzyme, a processed product of the microorganism or cell, and/or a culture liquid comprising the enzyme and obtained by culturing the microorganism or cell, to act on L-pipecolic acid as a substrate in the presence of 2-oxoglutaric acid and ferrous ion, wherein the L-pipecolic acid hydroxylase has the properties: (1) the enzyme can act on L-pipecolic acid in the presence of 2-oxoglutaric acid and ferrous ion to add a hydroxy group to the carbon atom at positions 3, 4, and/or 5 of L-pipecolic acid; and (2) the enzyme has a catalytic efficiency (kcat/Km) with L-proline that is equal to or less than 7 times the catalytic efficiency (kcat/Km) with L-pipecolic acid.

A minimally invasive device and method for suturing papillary muscles includes drawing a suture through a first papillary muscle using a needle, drawing the suture through a second papillary muscle, and tightening the suture to move at least one of the first papillary muscle and the second papillary muscle towards the other of the first papillary muscle and the second papillary muscle.

The present disclosure provides compositions and methods related to transcription factor systems. Such systems provide for modular and tunable protein expression driven by regulated transcriptional activity.

Provided are an amadoriase that is less likely to be influenced by oxygen concentration and a method and a reagent kit for measurement of HbA1c using such amadoriase. Provided are an amadoriase that is obtained via substitution of one or more amino acid residues at a position or positions corresponding to the position(s) selected from the group consisting of positions 280, 267, 269, 54, and 241 of the amadoriase derived from the genus Coniochaeta, a method for measurement of HbA1c, a reagent kit for measurement, and a sensor using such amadoriase. The modified amadoriase according to the invention has a lowered oxidase activity and an enhanced dehydrogenase activity, and this enables the use of an electron mediator, and this reduces the influence of oxygen concentration. Thus, HbA1c can be measured with high sensitivity.

The present disclosure relates to a variant polypeptide having attenuated dihydrodipicolinate reductase activity and a method of producing L-threonine using the same.

The present disclosure relates to a modified polypeptide, in which the activity of meso-diaminopimelate is weakened, and a method for producing L-threonine using the same.

MPO1 and MPO2 can be regulated for either decreasing or increasing alkaloid levels in plants, in particular in Nicotiana plants. In particular, suppressing or overexpressing one or more of MPO1 and MPO2 may be used to decrease or increase nicotine and nicotinic alkaloid levels in tobacco plants. Suppression or overexpression of one or more of MPO1 and MPO2 may be used in combination with modification of expression of other genes encoding enzymes on the nicotinic alkaloid biosynthetic pathway such as A622, NBB1, PMT, and QPT.

Genetically modified proteins with uricolytic activity are described. Proteins comprising truncated urate oxidases and methods for producing them, including PEGylated proteins comprising truncated urate oxidase are described.

Provided herein are CasX:gNA systems comprising CasX polypeptides, guide nucleic acids (gNA), and optionally donor template nucleic acids useful in the modification of a SOD1 gene. The systems are also useful for introduction into cells, for example eukaryotic cells having mutations in the SOD1 protein or the SOD1 regulatory element. Also provided are methods of using such CasX:gNA systems to modify cells having such mutations and utility in methods of treatment of a subject with a SOD1-related disease.

The present invention relates to a genetically engineered microorganism expressing (i) formate tetrahydrofolate (THF) ligase, methenyi-THF cyclohydrolase and methylene-THF dehydrogenase, (ii) the enzymes of the glycine cleavage system (GCS), (iii) serine deaminase and serine hydroxymethyltransferase (SHMT), (iv) an enzyme increasing the availability of NADPH, and (v) optionally formate dehydrogenase (FDH), and wherein the genetically engineered microorganism has been genetically engineered to express at least one of the enzymes of (i) to (v), wheren said enzyme is not expressed by the corresponding microorganism that has been used to prepare the genetically engineered microorganism, and wherein the enzymes of (i) to (v) are genomically expressed.