Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The microflora of 297 psoriasis patients was extensively examined. Throat, urine, and skin surfaces from scalp, ears, chest, face, axillary, submammary, umbilical, upper back, inguinal crease, gluteal-fold, perirectal, vaginal, pubis, penis, scrotal, leg, hands, feet, finger, and toenail areas were cultured for aerobic bacteria, yeast, and dermatophytes. Antibody levels to streptococcal enzymes were performed (streptolysin-O, DNAse-B, hyaluronidase, STREPTOZYME). Giemsa smears and KOH preparations were also used to determine yeast and dermatophyte presence. Associated organisms thought to provoke a psoriatic attack were as follows: streptococcal groups A, B, C, D, F, G, S viridans, S pneumoniae; Klebsiella pneumoniae, oxytoca; Escherichia coli; Enterobacter cloacae, E aerogenes, E agglomerans; Proteus mirabilis, P vulgaris; Citrobacter freundii, C diversus; Morganella morganii; Pseudomonas aeruginosa, P maltiphilia, P putida; Serratia marcescens; Acinetobacter calbio aceticus, A luoffi; Flavobacterium specie; CDC groups Ve-1, Ve-2, E-o2; Bacillus subtilis, cereus; Staphylococcus aureus; Candida albicans, C parapsilosis; Torulopsis, glabrata; Rhodotorula and dermatophytes. One or more antistreptococal enzyme tests was positive in 50% of patients. Titers to hepatitis E were elevated in one patient and to HIV in two patients.
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PMID:The role of microorganisms in psoriasis. 228 71

Chondroitin Sulfate ABC lyase I from Proteus vulgaris is an endolytic, broad-specificity glycosaminoglycan lyase, which degrades chondroitin, chondroitin-4-sulfate, dermatan sulfate, chondroitin-6-sulfate, and hyaluronan by beta-elimination of 1,4-hexosaminidic bond to unsaturated disaccharides and tetrasaccharides. Its structure revealed three domains. The N-terminal domain has a fold similar to that of carbohydrate-binding domains of xylanases and some lectins, the middle and C-terminal domains are similar to the structures of the two-domain chondroitin lyase AC and bacterial hyaluronidases. Although the middle domain shows a very low level of sequence identity with the catalytic domains of chondroitinase AC and hyaluronidase, the residues implicated in catalysis of the latter enzymes are present in chondroitinase ABC I. The substrate-binding site in chondroitinase ABC I is in a wide-open cleft, consistent with the endolytic action pattern of this enzyme. The tryptophan residues crucial for substrate binding in chondroitinase AC and hyaluronidases are lacking in chondroitinase ABC I. The structure of chondroitinase ABC I provides a framework for probing specific functions of active-site residues for understanding the remarkably broad specificity of this enzyme and perhaps engineering a desired specificity. The electron density map showed clearly that the deposited DNA sequence for residues 495-530 of chondroitin ABC lyase I, the segment containing two putative active-site residues, contains a frame-shift error resulting in an incorrectly translated amino acid sequence.
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PMID:Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution. 1270 21