Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.12.7.2 (hydrogenase)
 3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The first and the third steps in the aspartate biosynthesis pathway in Streptococcus bovis are catalyzed by two different forms of aspartokinase and a single homoserine dehydrogenase, respectively. These enzymes can be separated by ammonium sulfate fractionation and gel filtration on Sephadex G-200. The two aspartokinase isozymes differ in molecular weights and are subject to differential regulation. The aspartokinase system of S. bovis is characterized by the absence of specific negative allosteric effectors among the end products of the synthesis of amino acids of the aspartic family. Homoserine dehydrogenase, which catalyzes the third step of the aspartic family amino acid synthesis, also has such negative effectors as threonine and methionine. The aspartokinase isozymes do not form multienzyme complexes with homoserine hydrogenase in S. bovis.
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PMID:[Analysis of key enzyme activities involved in aspartate amino acid biosynthesis in Streptococcus bovis]. 811 40

The complete genome of the ammonia-oxidizing bacterium Nitrosospira multiformis (ATCC 25196(T)) consists of a circular chromosome and three small plasmids totaling 3,234,309 bp and encoding 2,827 putative proteins. Of the 2,827 putative proteins, 2,026 proteins have predicted functions and 801 are without conserved functional domains, yet 747 of these have similarity to other predicted proteins in databases. Gene homologs from Nitrosomonas europaea and Nitrosomonas eutropha were the best match for 42% of the predicted genes in N. multiformis. The N. multiformis genome contains three nearly identical copies of amo and hao gene clusters as large repeats. The features of N. multiformis that distinguish it from N. europaea include the presence of gene clusters encoding urease and hydrogenase, a ribulose-bisphosphate carboxylase/oxygenase-encoding operon of distinctive structure and phylogeny, and a relatively small complement of genes related to Fe acquisition. Systems for synthesis of a pyoverdine-like siderophore and for acyl-homoserine lactone were unique to N. multiformis among the sequenced genomes of ammonia-oxidizing bacteria. Gene clusters encoding proteins associated with outer membrane and cell envelope functions, including transporters, porins, exopolysaccharide synthesis, capsule formation, and protein sorting/export, were abundant. Numerous sensory transduction and response regulator gene systems directed toward sensing of the extracellular environment are described. Gene clusters for glycogen, polyphosphate, and cyanophycin storage and utilization were identified, providing mechanisms for meeting energy requirements under substrate-limited conditions. The genome of N. multiformis encodes the core pathways for chemolithoautotrophy along with adaptations for surface growth and survival in soil environments.
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PMID:Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing bacterium from the soil environment. 1839 Jun 76