WordNet

a dismissive term for a girl who is immature or who lacks respect; "she was incensed that this chit of a girl should dare to make a fool of her in front of the class"; "shes a saucy chit"
a tough semitransparent horny substance; the principal component of the exoskeletons of arthropods and the cell walls of certain fungi

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(飲食店の)請求伝票 / 短い手紙;メモ
子供;(特に生意気な)小娘
キチン質(節足動物の殻などを構成する角質の成分)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/19 10:01:58」(JST)

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In enzymology, a chitin synthase (EC 2.4.1.16) is an enzyme that catalyzes the chemical reaction

UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n⁺1

Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and [[[1,4-(N-acetyl-beta-D-glucosaminyl)]n]], whereas its two products are UDP and [[[1,4-(N-acetyl-beta-D-glucosaminyl)]n+1]].

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyl-transferase. Other names in common use include chitin-UDP N-acetylglucosaminyltransferase, chitin-uridine diphosphate acetylglucosaminyltransferase, chitin synthetase, and trans-N-acetylglucosaminosylase. This enzyme participates in aminosugars metabolism.

Production

Chitin Synthase is manufactured in the rough endoplasmic reticulum of fungi as the inactive form, zymogen. The zymogen is then packaged into chitosomes in the golgi apparatus. Chitosomes bring the zymogen to the hyphal tip of a mold or yeast cell membrane. Chitin synthase is placed into the interior side of the cell membrane and then activated.^{[citation needed]}

References

GLASER L, BROWN DH (1957). "The synthesis of chitin in cell-free extracts of Neurospora crassa". J. Biol. Chem. 228 (2): 729–42. PMID 13475355.
Sburlati A, Cabib E (1986). "Chitin synthetase 2, a presumptive participant in septum formation in Saccharomyces cerevisiae". J. Biol. Chem. 261 (32): 15147–52. PMID 2945823.

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English Journal

Evaluation of synthase and hemisynthase activities of glucosamine-6-phosphate synthase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Gaucher-Wieczorek F1, Guérineau V1, Touboul D2, Thétiot-Laurent S1, Pelissier F1, Badet-Denisot MA1, Badet B1, Durand P1.
Analytical biochemistry.Anal Biochem.2014 Aug 1;458:61-5. doi: 10.1016/j.ab.2014.04.033. Epub 2014 May 6.
Glucosamine-6-phosphate synthase (GlmS, EC 2.6.1.16) catalyzes the first and rate-limiting step in the hexosamine biosynthetic pathway, leading to the synthesis of uridine-5'-diphospho-N-acetyl-D-glucosamine, the major building block for the edification of peptidoglycan in bacteria, chitin in fungi,
PMID 24814295

DIETARY LUFENURON REDUCES EGG HATCH AND INFLUENCES PROTEIN EXPRESSION IN THE FRUIT FLY Bactrocera latifrons (HENDEL).

Chang CL1, Geib S, Cho IK, Li QX, Stanley D.
Archives of insect biochemistry and physiology.Arch Insect Biochem Physiol.2014 Aug;86(4):193-208. doi: 10.1002/arch.21169. Epub 2014 Apr 21.
Lufenuron (LFN), a chitin synthase inhibitor, impacts the fertility of Ceratitis capitata, Bactrocera dorsalis, B. cucurbitae, and B. latifrons. We posed the hypothesis that LFN curtails egg hatch in the solanaceous fruit fly, B. latifrons. In this study, newly emerged virgin adults were sexed and f
PMID 24753137

High resolution genetic mapping uncovers chitin synthase-1 as the target-site of the structurally diverse mite growth inhibitors clofentezine, hexythiazox and etoxazole in Tetranychus urticae.

Demaeght P1, Osborne EJ2, Odman-Naresh J3, Grbić M4, Nauen R5, Merzendorfer H3, Clark RM6, Van Leeuwen T7.
Insect biochemistry and molecular biology.Insect Biochem Mol Biol.2014 Aug;51:52-61. doi: 10.1016/j.ibmb.2014.05.004. Epub 2014 May 22.
The acaricides clofentezine, hexythiazox and etoxazole are commonly referred to as 'mite growth inhibitors', and clofentezine and hexythiazox have been used successfully for the integrated control of plant mite pests for decades. Although they are still important today, their mode of action has rema
PMID 24859419

Japanese Journal

Myosin Motor-Like Domain of Class VI Chitin Synthase CsmB of Aspergillus nidulans Is Not Functionally Equivalent to That of Class V Chitin Synthase CsmA

TSUIZAKI Makusu,OHTA Akinori,HORIUCHI Hiroyuki
Bioscience, biotechnology, and biochemistry 77(2), 369-374, 2013-02-23
NAID 10031164742

Myosin Motor-Like Domain of Class Ⅵ Chitin Synthase CsmB of Aspergillus nidulans Is Not Functionally Equivalent to That of Class Ⅴ Chitin Synthase CsmA

TSUIZAKI Makusu,OHTA Akinori,HORIUCHI Hiroyuki
Bioscience, Biotechnology, and Biochemistry 77(2), 369-374, 2013-02
NAID 40019593415

Myosin Motor-Like Domain of Class VI Chitin Synthase CsmB of Aspergillus nidulans Is Not Functionally Equivalent to That of Class V Chitin Synthase CsmA

TSUIZAKI Makusu,OHTA Akinori,HORIUCHI Hiroyuki
Bioscience, Biotechnology, and Biochemistry 77(2), 369-374, 2013
… Chitin is a major cell wall component of many filamentous fungi. … Among the eight chitin synthase genes of Aspergillus nidulans, csmA and csmB encode a myosin motor-like domain (MMD) and a chitin synthase domain (CSD) at their N- and C-termini respectively. …
NAID 130004138053

「キチン合成酵素」

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chitin synthase
Identifiers
EC number	2.4.1.16
CAS number	9030-18-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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PMC	articles
PubMed	articles
NCBI	proteins