Glycoside hydrolase family 19

In molecular biology, Glycoside hydrolase family 19 is a family of glycoside hydrolases.

Glycosyl hydrolases family 19
the refined crystal structure of an endochitinase from hordeum vulgare l. seeds to 1.8 angstroms resolution
Identifiers
SymbolGlyco_hydro_19
PfamPF00182
Pfam clanCL0037
InterProIPR000726
PROSITEPDOC00620
SCOPe2baa / SUPFAM
CAZyGH19
CDDcd00325

Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7] y[ _]9

Glycoside hydrolase family 19 CAZY GH_19 comprises enzymes with only one known activity; chitinase (EC 3.2.1.14).

Chitinases[8] are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitinases belong to glycoside hydrolase families 18 or 19.[9] Chitinases of family 19 (also known as classes IA or I and IB or II) are enzymes from plants that function in the defence against fungal and insect pathogens by destroying their chitin-containing cell wall. Class IA/I and IB/II enzymes differ in the presence (IA/I) or absence (IB/II) of a N-terminal chitin-binding domain. The catalytic domain of these enzymes consist of about 220 to 230 amino acid residues.

Active site
Active site of gycoside hydrolase family 19 papaya chitinase (PDB: 3cql​).[10] Conserved residues are shown surrounding the catalytic acid, Glu67. A GlcNAc2 unit binding in the -1 and +1 subsites is shown in narrow stick representation and an arrow indicates the position of the glycosidic oxygen.

GH19 enzymes has a conserved sequence motif ([FHY]-G-R-G-[AP]-ζ-Q-[IL]-[ST]-[FHYW]-[HN]-[FY]-[NY], ζ= hydrophilic amino acid) in its active site.[11]

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gollark: ```python#!/usr/bin/env python3import argparseimport subprocessimport randomimport stringparser = argparse.ArgumentParser(description="Compile a WHY program using WHYJIT.")parser.add_argument("input", help="File containing WHY source code")parser.add_argument("-o", "--output", help="Filename of the output executable to make", default="./a.why")parser.add_argument("-O", "--optimize", help="Optimization level", type=int, default="0")args = parser.parse_args()def randomword(length): letters = string.ascii_lowercase return ''.join(random.choice(letters) for i in range(length))def which(program): proc = subprocess.run(["which", program], stdout=subprocess.PIPE) if proc.returncode == 0: return proc.stdout.replace(b"\n", b"") else: return Nonedef find_C_compiler(): compilers = ["gcc", "clang", "tcc", "cc"] for compiler in compilers: path = which(compiler) if path != None: return pathdef build_output(code, mx): C_code = f"""#define QUITELONG long long intconst QUITELONG max = {mx};int main() {{ volatile QUITELONG i = 0; // disable some "optimizations" that RUIN OUR BEAUTIFUL CODE! while (i < max) {{ i++; }} {code}}} """ heredoc = randomword(100) devnull = "2>/dev/null" shell_script = f"""#!/bin/shTMP1=/tmp/ignore-meTMP2=/tmp/ignore-me-tooTMP3=/tmp/dont-look-here cat << {heredoc} > $TMP1{C_code}{heredoc}sed -e '1,/^exit \$?$/d' "$0" > $TMP3chmod +x $TMP3$TMP3 -x c -o $TMP2 $TMP1chmod +x $TMP2$TMP2exit $?""".encode("utf-8") with open(find_C_compiler(), "rb") as f: return shell_script + f.read()input = args.inputoutput = args.outputwith open(input, "r") as f: contents = f.read() looplen = max(1000, (2 ** -args.optimize) * 1000000000) code = build_output( contents, looplen ) with open(output, "wb") as out: out.write(code)```
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References
  1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. Bibcode:1995PNAS...92.7090H. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
  2. Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
  3. Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 ( Pt 2) (Pt 2): 695–6. doi:10.1042/bj3160695. PMC 1217404. PMID 8687420.
  4. "Home". CAZy.org. Retrieved 2018-03-06.
  5. Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490-5. doi:10.1093/nar/gkt1178. PMC 3965031. PMID 24270786.
  6. "Glycoside Hydrolase Family 19". CAZypedia.org. Retrieved 2018-03-06.
  7. CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. PMID 29040563.
  8. Flach J, Pilet PE, Jollès P (August 1992). "What's new in chitinase research?". Experientia. 48 (8): 701–16. doi:10.1007/BF02124285. PMID 1516675.
  9. Henrissat B (December 1991). "A classification of glycosyl hydrolases based on amino acid sequence similarities". The Biochemical Journal. 280 ( Pt 2) (2): 309–16. doi:10.1042/bj2800309. PMC 1130547. PMID 1747104.
  10. Eijsink V, Hoell I, Vaaje-Kolstada G (2010-01-01). "Structure and function of enzymes acting on chitin and chitosan". Biotechnology & Genetic Engineering Reviews. 27 (1): 331–66. doi:10.1080/02648725.2010.10648156. PMID 21415904.
  11. Udaya Prakash NA, Jayanthi M, Sabarinathan R, Kangueane P, Mathew L, Sekar K (May 2010). "Evolution, homology conservation, and identification of unique sequence signatures in GH19 family chitinases". Journal of Molecular Evolution. 70 (5): 466–78. Bibcode:2010JMolE..70..466U. doi:10.1007/s00239-010-9345-z. PMID 20480157.
This article incorporates text from the public domain Pfam and InterPro: IPR000726
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