Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp.

The crystal structure of a cold-active alkaline phosphatase from a psychrophile, Shewanella sp. (SCAP), was solved at 2.2 A.

Characterisitics and gene cloning of phospholipase D of the psychrophile, Shewanella sp.

Phospholipase D, with a molecular mass of 64 kDa, was purified from the psychrophile, Shewanella sp. The enzyme showed maximal activity at pH 7.8 and 40 degrees C in the presence of the Ca2+-ion, and its activity at 10 degrees C was 6.

Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp.

The cold-active protein-tyrosine phosphatase (CAPTPase) of a psychrophile, Shewanella sp., shows high catalytic activity below 20 degrees C. The catalytic residue of CAPTPase is histidine, as opposed to the cysteine of known protein-tyrosine phosphatases (PTPases), and the enzyme protein has three amino acid sequences, Asp-Xaa-His, Gly-Asp-Xaa-Xaa-Asp-Arg and Gly-Asn-His-Glu, that are observed in many protein-serine/threonine phosphatases (PS/TPases).

Expression of cytochrome c oxidase subunit 1 gene in the brain at an early stage in the termination of pupal diapause in the sweet potato hornworm, Agrius convolvuli.

Suppression-subtractive hybridization was used to isolate cDNAs specifically expressed in the brain at the termination of pupal diapause in Agrius convolvuli. One of the isolated clones shows similarity to the cytochrome c oxidase subunit 1 (COX1) gene. The full-length cDNA was obtained from brain mRNA by rapid amplification of cDNA ends (RACE).

Specification of amino acid residues essential for the catalytic reaction of cold-active protein-tyrosine phosphatase of a psychrophile, Shewanella sp.

Protein-tyrosine phosphatase [EC 3.1.3.

Catalytic efficiency and some structural properties of cold-active protein-tyrosine-phosphatase.

A procedure was established for expression and purification of abundant recombinant cold-active protein-tyrosine-phosphatase (RCPTPase), which showed identical enzymatic characteristics to the native enzyme (NCPTPase). The purified RCPTPase showed high catalytic activity at low temperature and maximal activity at 30 degrees C. RCPTPase has a thermodynamic characteristic in that its activation enthalpy was determined to be low, 4.

Crystallization and preliminary X-ray studies of cold-active protein-tyrosine phosphatase of Shewanella sp.

Cold-active protein-tyrosine phosphatase (PTPase) of Shewanella sp. was expressed, purified and crystallized using the hanging-drop vapour-diffusion method at two different pH values (4.6 and 8.

Purification and characterization of nucleoside diphosphate kinase from the brain of Bombyx mori.

Nucleoside diphosphate kinase in the brain of Bombyx mori was purified by ammonium sulfate fractionation, and a sequence of chromatographies on DEAE-Cellulofine, hydroxyapatite, Mono-S, and Mono-Q column. The purified enzyme preparation was found to be electrophoretically homogeneous on SDS-PAGE, and its molecular mass was determined to be 18 kDa. The purified protein was digested and the amino acid sequences of resulting peptides were determined.

Cloning of cold-active alkaline phosphatase gene of a psychrophile, Shewanella sp., and expression of the recombinant enzyme.

A psychrophilic alkaline phosphatase (EC 3.1.3.

TGTCACA motif is a novel cis-regulatory enhancer element involved in fruit-specific expression of the cucumisin gene.

Cucumisin, a subtilisin-like serine protease, is expressed at high levels in the fruit of melon (Cucumis melo L.) and accumulates in the juice. We investigated roles of the promoter regions and DNA-protein interactions in fruit-specific expression of the cucumisin gene.